TY  - JOUR
AU  - Zhou, Qingwen
AU  - Holloman, William K.
AU  - Kojić, Milorad
PY  - 2018
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1138
AB  - Primary components of the homologous recombination pathway in eukaryotes include Rad51 whose function is to search for DNA sequence homology and promote strand exchange, its mediator BRCA2, and Dss1, a key regulator of BRCA2. We seek to understand the role of BRCA2 in governing the activity of Rad51 and to learn how BRCA2 function is regulated by Dss1. We use the microbe Ustilago maydis as a model system for experimentation because it has a well-conserved BRCA2-homolog, Brh2, and is amenable to biochemical and molecular genetic manipulations and analysis. The powerful attributes of this system open the way for gaining insight into BRCA2's molecular mechanism through avenues not immediately approachable in the vertebrate systems. Here we provide protocols for preparing Brh2, Dss1, and Rad51 as reagents for use in biochemical assays to monitor function and present methods for transposon-based mutational analysis of Brh2 for use in genetic dissection of function.
PB  - Elsevier Academic Press Inc, San Diego
T2  - Mechanisms of Dna Recombination and Genome Rearrangements: Methods To Study Homologous Recombination
T1  - Approaches to Understanding the Mediator Function of Brh2 in Ustilago maydis
EP  - 525
SP  - 513
VL  - 600
DO  - 10.1016/bs.mie.2017.11.019
ER  - 

@article{
author = "Zhou, Qingwen and Holloman, William K. and Kojić, Milorad",
year = "2018",
abstract = "Primary components of the homologous recombination pathway in eukaryotes include Rad51 whose function is to search for DNA sequence homology and promote strand exchange, its mediator BRCA2, and Dss1, a key regulator of BRCA2. We seek to understand the role of BRCA2 in governing the activity of Rad51 and to learn how BRCA2 function is regulated by Dss1. We use the microbe Ustilago maydis as a model system for experimentation because it has a well-conserved BRCA2-homolog, Brh2, and is amenable to biochemical and molecular genetic manipulations and analysis. The powerful attributes of this system open the way for gaining insight into BRCA2's molecular mechanism through avenues not immediately approachable in the vertebrate systems. Here we provide protocols for preparing Brh2, Dss1, and Rad51 as reagents for use in biochemical assays to monitor function and present methods for transposon-based mutational analysis of Brh2 for use in genetic dissection of function.",
publisher = "Elsevier Academic Press Inc, San Diego",
journal = "Mechanisms of Dna Recombination and Genome Rearrangements: Methods To Study Homologous Recombination",
title = "Approaches to Understanding the Mediator Function of Brh2 in Ustilago maydis",
pages = "525-513",
volume = "600",
doi = "10.1016/bs.mie.2017.11.019"
}

Zhou, Q., Holloman, W. K.,& Kojić, M.. (2018). Approaches to Understanding the Mediator Function of Brh2 in Ustilago maydis. in Mechanisms of Dna Recombination and Genome Rearrangements: Methods To Study Homologous Recombination
Elsevier Academic Press Inc, San Diego., 600, 513-525.
https://doi.org/10.1016/bs.mie.2017.11.019

Zhou Q, Holloman WK, Kojić M. Approaches to Understanding the Mediator Function of Brh2 in Ustilago maydis. in Mechanisms of Dna Recombination and Genome Rearrangements: Methods To Study Homologous Recombination. 2018;600:513-525.
doi:10.1016/bs.mie.2017.11.019 .

Zhou, Qingwen, Holloman, William K., Kojić, Milorad, "Approaches to Understanding the Mediator Function of Brh2 in Ustilago maydis" in Mechanisms of Dna Recombination and Genome Rearrangements: Methods To Study Homologous Recombination, 600 (2018):513-525,
https://doi.org/10.1016/bs.mie.2017.11.019 . .

TY  - JOUR
AU  - Zhou, Qingwen
AU  - Kojić, Milorad
AU  - Holloman, William K.
PY  - 2012
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/610
AB  - Dss1 is an intrinsically unstructured polypeptide that partners with the much larger Brh2 protein, the BRCA2 ortholog in Ustilago maydis, to form a tight complex. Mutants lacking Dss1 have essentially the same phenotype as mutants defective in Brh2, implying that through physical interaction Dss1 serves as a positive activator of Brh2. Dss1 associates with Brh2 through an interaction surface in the carboxy-terminal region. Certain derivatives of Brh2 lacking this interaction surface remain highly competent in DNA repair as long as a DNA-binding domain is present. However, the Dss1-independent activity raises the question of what function might be met in the native protein by having Brh2 under Dss1 control. Using a set of Brh2 fusions and truncated derivatives, we show here that Dss1 is capable of exerting control when there is a cognate Dss1-interacting surface present. We find that association of Dss1 attenuates the DNA binding potential of Brh2 and that the ammo terminal domain of Brh2 helps evict Dss1 from its carboxy-terminal interaction surface. The findings presented here add to the notion that Dss1 serves in a regulatory capacity to dictate order in association of Brh2's amino terminal and carboxyterminal domains with DNA.
PB  - Amer Chemical Soc, Washington
T2  - Biochemistry
T1  - Dss1 Release Activates DNA Binding Potential in Brh2
EP  - 9146
IS  - 45
SP  - 9137
VL  - 51
DO  - 10.1021/bi3011187
ER  - 

@article{
author = "Zhou, Qingwen and Kojić, Milorad and Holloman, William K.",
year = "2012",
abstract = "Dss1 is an intrinsically unstructured polypeptide that partners with the much larger Brh2 protein, the BRCA2 ortholog in Ustilago maydis, to form a tight complex. Mutants lacking Dss1 have essentially the same phenotype as mutants defective in Brh2, implying that through physical interaction Dss1 serves as a positive activator of Brh2. Dss1 associates with Brh2 through an interaction surface in the carboxy-terminal region. Certain derivatives of Brh2 lacking this interaction surface remain highly competent in DNA repair as long as a DNA-binding domain is present. However, the Dss1-independent activity raises the question of what function might be met in the native protein by having Brh2 under Dss1 control. Using a set of Brh2 fusions and truncated derivatives, we show here that Dss1 is capable of exerting control when there is a cognate Dss1-interacting surface present. We find that association of Dss1 attenuates the DNA binding potential of Brh2 and that the ammo terminal domain of Brh2 helps evict Dss1 from its carboxy-terminal interaction surface. The findings presented here add to the notion that Dss1 serves in a regulatory capacity to dictate order in association of Brh2's amino terminal and carboxyterminal domains with DNA.",
publisher = "Amer Chemical Soc, Washington",
journal = "Biochemistry",
title = "Dss1 Release Activates DNA Binding Potential in Brh2",
pages = "9146-9137",
number = "45",
volume = "51",
doi = "10.1021/bi3011187"
}

Zhou, Q., Kojić, M.,& Holloman, W. K.. (2012). Dss1 Release Activates DNA Binding Potential in Brh2. in Biochemistry
Amer Chemical Soc, Washington., 51(45), 9137-9146.
https://doi.org/10.1021/bi3011187

Zhou Q, Kojić M, Holloman WK. Dss1 Release Activates DNA Binding Potential in Brh2. in Biochemistry. 2012;51(45):9137-9146.
doi:10.1021/bi3011187 .

Zhou, Qingwen, Kojić, Milorad, Holloman, William K., "Dss1 Release Activates DNA Binding Potential in Brh2" in Biochemistry, 51, no. 45 (2012):9137-9146,
https://doi.org/10.1021/bi3011187 . .

TY  - JOUR
AU  - Kojić, Milorad
AU  - Zhou, Qingwen
AU  - Fan, Jie
AU  - Holloman, William K.
PY  - 2011
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/476
AB  - Brh2, a member of the BRCA2 family of proteins, governs homologous recombination in the fungus Ustilago maydis through interaction with Rad51. Brh2 serves at an early step in homologous recombination to mediate Rad51 nucleoprotein filament formation and also has the capability to function at a later step in recombination through its inherent DNA annealing activity. Rec2, a Rad51 paralogue, and Rad52 are additional components of the homologous recombination system, but the absence of either is less critical than Brh2 for operational activity. Here we tested a variety of mutant forms of Brh2 for activity in recombinational repair as measured by DNA repair proficiency. We found that a mutant of Brh2 deleted of the non-canonical DNA-binding domain within the N-terminal region is dependent upon the presence of Rad52 for DNA repair activity. We also determined that a motif first identified in human BRCA2 as important in binding DMC1 also contributes to DNA repair proficiency and cooperates with the BRC element in Rad51 binding.
PB  - Wiley, Hoboken
T2  - Molecular Microbiology
T1  - Mutational analysis of Brh2 reveals requirements for compensating mediator functions
EP  - 191
IS  - 1
SP  - 180
VL  - 79
DO  - 10.1111/j.1365-2958.2010.07440.x
ER  - 

@article{
author = "Kojić, Milorad and Zhou, Qingwen and Fan, Jie and Holloman, William K.",
year = "2011",
abstract = "Brh2, a member of the BRCA2 family of proteins, governs homologous recombination in the fungus Ustilago maydis through interaction with Rad51. Brh2 serves at an early step in homologous recombination to mediate Rad51 nucleoprotein filament formation and also has the capability to function at a later step in recombination through its inherent DNA annealing activity. Rec2, a Rad51 paralogue, and Rad52 are additional components of the homologous recombination system, but the absence of either is less critical than Brh2 for operational activity. Here we tested a variety of mutant forms of Brh2 for activity in recombinational repair as measured by DNA repair proficiency. We found that a mutant of Brh2 deleted of the non-canonical DNA-binding domain within the N-terminal region is dependent upon the presence of Rad52 for DNA repair activity. We also determined that a motif first identified in human BRCA2 as important in binding DMC1 also contributes to DNA repair proficiency and cooperates with the BRC element in Rad51 binding.",
publisher = "Wiley, Hoboken",
journal = "Molecular Microbiology",
title = "Mutational analysis of Brh2 reveals requirements for compensating mediator functions",
pages = "191-180",
number = "1",
volume = "79",
doi = "10.1111/j.1365-2958.2010.07440.x"
}

Kojić, M., Zhou, Q., Fan, J.,& Holloman, W. K.. (2011). Mutational analysis of Brh2 reveals requirements for compensating mediator functions. in Molecular Microbiology
Wiley, Hoboken., 79(1), 180-191.
https://doi.org/10.1111/j.1365-2958.2010.07440.x

Kojić M, Zhou Q, Fan J, Holloman WK. Mutational analysis of Brh2 reveals requirements for compensating mediator functions. in Molecular Microbiology. 2011;79(1):180-191.
doi:10.1111/j.1365-2958.2010.07440.x .

Kojić, Milorad, Zhou, Qingwen, Fan, Jie, Holloman, William K., "Mutational analysis of Brh2 reveals requirements for compensating mediator functions" in Molecular Microbiology, 79, no. 1 (2011):180-191,
https://doi.org/10.1111/j.1365-2958.2010.07440.x . .

TY  - JOUR
AU  - Kojić, Milorad
AU  - Zhou, Qingwen
AU  - Fan, Jie
AU  - Holloman, William K.
PY  - 2011
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1619
AB  - Brh2, a member of the BRCA2 family of proteins, governs homologous recombination in the
fungus Ustilago maydis through interaction with Rad51. Brh2 serves at an early step in
homologous recombination to mediate Rad51 nucleoprotein filament formation and also has the
capability to function at a later step in recombination through its inherent DNA annealing activity.
Rec2, a Rad51 paralog, and Rad52, are additional components of the homologous recombination
system, but the absence of either is less critical than Brh2 for operational activity. Here we tested a
variety of mutant forms of Brh2 for activity in recombinational repair as measured by DNA repair
proficiency. We found that a mutant of Brh2 deleted of the non-canonical DNA-binding domain
within the N-terminal region is dependent upon the presence of Rad52 for DNA-repair activity.
We also determined that a motif first identified in human BRCA2 as important in binding DMC1
also contributes to DNA repair proficiency and cooperates with the BRC element in Rad51
binding.
PB  - Wiley, Hoboken
T2  - Molecular Microbiology
T1  - Mutational analysis of Brh2 reveals requirements for compensating mediator functions
EP  - 191
IS  - 1
SP  - 180
VL  - 79
DO  - 10.1111/j.1365-2958.2010.07440.x
ER  - 

@article{
author = "Kojić, Milorad and Zhou, Qingwen and Fan, Jie and Holloman, William K.",
year = "2011",
abstract = "Brh2, a member of the BRCA2 family of proteins, governs homologous recombination in the
fungus Ustilago maydis through interaction with Rad51. Brh2 serves at an early step in
homologous recombination to mediate Rad51 nucleoprotein filament formation and also has the
capability to function at a later step in recombination through its inherent DNA annealing activity.
Rec2, a Rad51 paralog, and Rad52, are additional components of the homologous recombination
system, but the absence of either is less critical than Brh2 for operational activity. Here we tested a
variety of mutant forms of Brh2 for activity in recombinational repair as measured by DNA repair
proficiency. We found that a mutant of Brh2 deleted of the non-canonical DNA-binding domain
within the N-terminal region is dependent upon the presence of Rad52 for DNA-repair activity.
We also determined that a motif first identified in human BRCA2 as important in binding DMC1
also contributes to DNA repair proficiency and cooperates with the BRC element in Rad51
binding.",
publisher = "Wiley, Hoboken",
journal = "Molecular Microbiology",
title = "Mutational analysis of Brh2 reveals requirements for compensating mediator functions",
pages = "191-180",
number = "1",
volume = "79",
doi = "10.1111/j.1365-2958.2010.07440.x"
}

Kojić, M., Zhou, Q., Fan, J.,& Holloman, W. K.. (2011). Mutational analysis of Brh2 reveals requirements for compensating mediator functions. in Molecular Microbiology
Wiley, Hoboken., 79(1), 180-191.
https://doi.org/10.1111/j.1365-2958.2010.07440.x

Kojić M, Zhou Q, Fan J, Holloman WK. Mutational analysis of Brh2 reveals requirements for compensating mediator functions. in Molecular Microbiology. 2011;79(1):180-191.
doi:10.1111/j.1365-2958.2010.07440.x .

Kojić, Milorad, Zhou, Qingwen, Fan, Jie, Holloman, William K., "Mutational analysis of Brh2 reveals requirements for compensating mediator functions" in Molecular Microbiology, 79, no. 1 (2011):180-191,
https://doi.org/10.1111/j.1365-2958.2010.07440.x . .

TY  - JOUR
AU  - Zhou, Qingwen
AU  - Kojić, Milorad
AU  - Holloman, William K.
PY  - 2009
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/360
AB  - The C-terminal region of Brh2 (Brh2(CT)), the BRCA2 homolog in Ustilago maydis, is highly conserved and aligns with the DSS1/DNA-binding domain (DBD) of mammalian BRCA2, while the N-terminal region (Brh2(NT)) is poorly conserved and has no obvious functional domain except for the single Rad51-interacting BRC element. Paradoxically, Brh2(NT), but not Brh2(CT), complements the DNA repair and recombination deficiency of the brh2 mutant. We show here that Brh2(NT) exhibits an unexpected DNA binding activity with properties similar to that of the full-length protein. Deletion mapping localized the region responsible for the DNA binding activity to a stretch of residues between the BRC element and the canonical DBD. A heterologous DNA-binding domain from the large subunit of replication protein A substituted for the endogenous binding region within Brh2(NT) in supporting DNA repair. Rad51-promoted strand invasion was stimulated by Brh2(NT), but required the presence of the BRC element. The findings suggest a model in which Brh2(NT) serves as the principal site for association with DNA, while the Brh2(CT) provides a means for regulation.
PB  - Amer Soc Biochemistry Molecular Biology Inc, Bethesda
T2  - Journal of Biological Chemistry
T1  - DNA-binding Domain within the Brh2 N Terminus Is the Primary Interaction Site for Association with DNA
EP  - 8273
IS  - 13
SP  - 8265
VL  - 284
DO  - 10.1074/jbc.M809226200
ER  - 

@article{
author = "Zhou, Qingwen and Kojić, Milorad and Holloman, William K.",
year = "2009",
abstract = "The C-terminal region of Brh2 (Brh2(CT)), the BRCA2 homolog in Ustilago maydis, is highly conserved and aligns with the DSS1/DNA-binding domain (DBD) of mammalian BRCA2, while the N-terminal region (Brh2(NT)) is poorly conserved and has no obvious functional domain except for the single Rad51-interacting BRC element. Paradoxically, Brh2(NT), but not Brh2(CT), complements the DNA repair and recombination deficiency of the brh2 mutant. We show here that Brh2(NT) exhibits an unexpected DNA binding activity with properties similar to that of the full-length protein. Deletion mapping localized the region responsible for the DNA binding activity to a stretch of residues between the BRC element and the canonical DBD. A heterologous DNA-binding domain from the large subunit of replication protein A substituted for the endogenous binding region within Brh2(NT) in supporting DNA repair. Rad51-promoted strand invasion was stimulated by Brh2(NT), but required the presence of the BRC element. The findings suggest a model in which Brh2(NT) serves as the principal site for association with DNA, while the Brh2(CT) provides a means for regulation.",
publisher = "Amer Soc Biochemistry Molecular Biology Inc, Bethesda",
journal = "Journal of Biological Chemistry",
title = "DNA-binding Domain within the Brh2 N Terminus Is the Primary Interaction Site for Association with DNA",
pages = "8273-8265",
number = "13",
volume = "284",
doi = "10.1074/jbc.M809226200"
}

Zhou, Q., Kojić, M.,& Holloman, W. K.. (2009). DNA-binding Domain within the Brh2 N Terminus Is the Primary Interaction Site for Association with DNA. in Journal of Biological Chemistry
Amer Soc Biochemistry Molecular Biology Inc, Bethesda., 284(13), 8265-8273.
https://doi.org/10.1074/jbc.M809226200

Zhou Q, Kojić M, Holloman WK. DNA-binding Domain within the Brh2 N Terminus Is the Primary Interaction Site for Association with DNA. in Journal of Biological Chemistry. 2009;284(13):8265-8273.
doi:10.1074/jbc.M809226200 .

Zhou, Qingwen, Kojić, Milorad, Holloman, William K., "DNA-binding Domain within the Brh2 N Terminus Is the Primary Interaction Site for Association with DNA" in Journal of Biological Chemistry, 284, no. 13 (2009):8265-8273,
https://doi.org/10.1074/jbc.M809226200 . .

TY  - JOUR
AU  - Zhou, Qingwen
AU  - Mazloum, Nayef
AU  - Mao, Ninghui
AU  - Kojić, Milorad
AU  - Holloman, William K.
PY  - 2009
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/379
AB  - Brh2, the BRCA2 homologue in Ustilago maydis, plays a crucial role in homologous recombination by controlling Rad51. In turn, Brh2 is governed by Dss1, an intrinsically disordered protein that forms a tight complex with the C-terminal region of Brh2. This region of the protein associating with Dss1 is highly conserved in sequence and by comparison with mammalian BRCA2 corresponds to a part of the DNA binding domain with characteristic OB folds. The N-terminal region of Brh2 harbors a less-defined but powerful DNA binding site, the activity of which is revealed upon deletion of the C-terminal region. Full-length Brh2 complexed with Dss1 binds DNA slowly, while the N-terminal fragment binds quickly. The DNA binding activity of full-length Brh2 appears to correlate with dissociation of Dss1. Addition of Dss1 to the heterotypic Brh2-Dss1 complex attenuates DNA binding activity, but not by direct competition for the N-terminal DNA binding site. Conversely, the Brh2-Dss1 complex dissociates more quickly when DNA is present. These findings suggest a model in which binding of Brh2 to DNA is subject to allosteric regulation by Dss1.
PB  - Amer Chemical Soc, Washington
T2  - Biochemistry
T1  - Dss1 Regulates Interaction of Brh2 with DNA
EP  - 11938
IS  - 50
SP  - 11929
VL  - 48
DO  - 10.1021/bi901775j
ER  - 

@article{
author = "Zhou, Qingwen and Mazloum, Nayef and Mao, Ninghui and Kojić, Milorad and Holloman, William K.",
year = "2009",
abstract = "Brh2, the BRCA2 homologue in Ustilago maydis, plays a crucial role in homologous recombination by controlling Rad51. In turn, Brh2 is governed by Dss1, an intrinsically disordered protein that forms a tight complex with the C-terminal region of Brh2. This region of the protein associating with Dss1 is highly conserved in sequence and by comparison with mammalian BRCA2 corresponds to a part of the DNA binding domain with characteristic OB folds. The N-terminal region of Brh2 harbors a less-defined but powerful DNA binding site, the activity of which is revealed upon deletion of the C-terminal region. Full-length Brh2 complexed with Dss1 binds DNA slowly, while the N-terminal fragment binds quickly. The DNA binding activity of full-length Brh2 appears to correlate with dissociation of Dss1. Addition of Dss1 to the heterotypic Brh2-Dss1 complex attenuates DNA binding activity, but not by direct competition for the N-terminal DNA binding site. Conversely, the Brh2-Dss1 complex dissociates more quickly when DNA is present. These findings suggest a model in which binding of Brh2 to DNA is subject to allosteric regulation by Dss1.",
publisher = "Amer Chemical Soc, Washington",
journal = "Biochemistry",
title = "Dss1 Regulates Interaction of Brh2 with DNA",
pages = "11938-11929",
number = "50",
volume = "48",
doi = "10.1021/bi901775j"
}

Zhou, Q., Mazloum, N., Mao, N., Kojić, M.,& Holloman, W. K.. (2009). Dss1 Regulates Interaction of Brh2 with DNA. in Biochemistry
Amer Chemical Soc, Washington., 48(50), 11929-11938.
https://doi.org/10.1021/bi901775j

Zhou Q, Mazloum N, Mao N, Kojić M, Holloman WK. Dss1 Regulates Interaction of Brh2 with DNA. in Biochemistry. 2009;48(50):11929-11938.
doi:10.1021/bi901775j .

Zhou, Qingwen, Mazloum, Nayef, Mao, Ninghui, Kojić, Milorad, Holloman, William K., "Dss1 Regulates Interaction of Brh2 with DNA" in Biochemistry, 48, no. 50 (2009):11929-11938,
https://doi.org/10.1021/bi901775j . .

TY  - JOUR
AU  - Kojić, Milorad
AU  - Mao, Ninghui
AU  - Zhou, Qingwen
AU  - Lisby, Michael
AU  - Holloman, William K.
PY  - 2008
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/314
AB  - A single Rad52-related protein is evident by blast analysis of the Ustilago maydis genome database. Mutants created by disruption of the structural gene exhibited few discernible defects in resistance to UV, ionizing radiation, chemical alkylating or cross-linking agents. No deficiency was noted in spontaneous mutator activity, allelic recombination or meiosis. GFP-Rad51 foci were formed in rad52 cells following DNA damage, but were initially less intense than normal suggesting a possible role for Rad52 in formation of the Rad51 nucleoprotein filament. A search for interacting genes that confer a synthetic fitness phenotype with rad52 after DNA damage by UV irradiation identified the genes for Mph1, Ercc1 and the Rad51 paralogue Rec2. Testing known mutants in recombinational repair revealed an additional interaction with the BRCA2 orthologue Brh2. Suppression of the rec2 mutant's UV sensitivity by overexpressing Brh2 was found to be dependent on Rad52. The results suggest that Rad52 serves in an overlapping, compensatory role with both Rec2 and Brh2 to promote and maintain formation of the Rad51 nucleoprotein filament.
PB  - Wiley, Hoboken
T2  - Molecular Microbiology
T1  - Compensatory role for Rad52 during recombinational repair in Ustilago maydis
EP  - 1168
IS  - 5
SP  - 1156
VL  - 67
DO  - 10.1111/j.1365-2958.2008.06116.x
ER  - 

@article{
author = "Kojić, Milorad and Mao, Ninghui and Zhou, Qingwen and Lisby, Michael and Holloman, William K.",
year = "2008",
abstract = "A single Rad52-related protein is evident by blast analysis of the Ustilago maydis genome database. Mutants created by disruption of the structural gene exhibited few discernible defects in resistance to UV, ionizing radiation, chemical alkylating or cross-linking agents. No deficiency was noted in spontaneous mutator activity, allelic recombination or meiosis. GFP-Rad51 foci were formed in rad52 cells following DNA damage, but were initially less intense than normal suggesting a possible role for Rad52 in formation of the Rad51 nucleoprotein filament. A search for interacting genes that confer a synthetic fitness phenotype with rad52 after DNA damage by UV irradiation identified the genes for Mph1, Ercc1 and the Rad51 paralogue Rec2. Testing known mutants in recombinational repair revealed an additional interaction with the BRCA2 orthologue Brh2. Suppression of the rec2 mutant's UV sensitivity by overexpressing Brh2 was found to be dependent on Rad52. The results suggest that Rad52 serves in an overlapping, compensatory role with both Rec2 and Brh2 to promote and maintain formation of the Rad51 nucleoprotein filament.",
publisher = "Wiley, Hoboken",
journal = "Molecular Microbiology",
title = "Compensatory role for Rad52 during recombinational repair in Ustilago maydis",
pages = "1168-1156",
number = "5",
volume = "67",
doi = "10.1111/j.1365-2958.2008.06116.x"
}

Kojić, M., Mao, N., Zhou, Q., Lisby, M.,& Holloman, W. K.. (2008). Compensatory role for Rad52 during recombinational repair in Ustilago maydis. in Molecular Microbiology
Wiley, Hoboken., 67(5), 1156-1168.
https://doi.org/10.1111/j.1365-2958.2008.06116.x

Kojić M, Mao N, Zhou Q, Lisby M, Holloman WK. Compensatory role for Rad52 during recombinational repair in Ustilago maydis. in Molecular Microbiology. 2008;67(5):1156-1168.
doi:10.1111/j.1365-2958.2008.06116.x .

Kojić, Milorad, Mao, Ninghui, Zhou, Qingwen, Lisby, Michael, Holloman, William K., "Compensatory role for Rad52 during recombinational repair in Ustilago maydis" in Molecular Microbiology, 67, no. 5 (2008):1156-1168,
https://doi.org/10.1111/j.1365-2958.2008.06116.x . .

TY  - JOUR
AU  - Mao, Ninghui
AU  - Zhou, Qingwen
AU  - Kojić, Milorad
AU  - Perez-Martin, Jose
AU  - Holloman, William K.
PY  - 2007
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1616
AB  - The BRCA2 tumor suppressor functions in repair of DNA by homologous recombination through regulating the action of Rad51. In turn, BRCA2 appears to be regulated by other interacting proteins. Dss1, a small interacting protein that binds to the C-terminal domain, has a profound effect on activity as deduced from studies on the BRCA2-related protein Brh2 in Ustilago maydis. Evidence accumulating in mammalian systems suggests that BCCIP, another small interacting protein that binds to the C-terminal domain of BRCA2, also serves to regulate homologous recombination activity. Here we were interested in testing the role of the putative U. maydis BCCIP ortholog Bcp1 in DNA repair and recombination. In keeping with the mammalian paradigm, Bcp1 bound to the C-terminal region of Brh2. Mutants deleted of the gene were extremely slow growing, showed a delay passing through S phase and exhibited sensitivity to hydroxyurea, but were other-wise normal in DNA repair and homologous recombination. In the absence of Bcp1 cells were unable to maintain the wild type morphology when challenged by a DNA replication stress. These results suggest that Bcp1 could be involved in coordinating morphogenetic events with DNA processing during replication.
PB  - Elsevier, Amsterdam
T2  - DNA Repair
T1  - Ortholog of BRCA2-interacting protein BCCIP controls morphogenetic responses during DNA replication stress in Ustilago maydis
EP  - 1660
IS  - 11
SP  - 1651
VL  - 6
DO  - 10.1016/j.dnarep.2007.05.012
ER  - 

@article{
author = "Mao, Ninghui and Zhou, Qingwen and Kojić, Milorad and Perez-Martin, Jose and Holloman, William K.",
year = "2007",
abstract = "The BRCA2 tumor suppressor functions in repair of DNA by homologous recombination through regulating the action of Rad51. In turn, BRCA2 appears to be regulated by other interacting proteins. Dss1, a small interacting protein that binds to the C-terminal domain, has a profound effect on activity as deduced from studies on the BRCA2-related protein Brh2 in Ustilago maydis. Evidence accumulating in mammalian systems suggests that BCCIP, another small interacting protein that binds to the C-terminal domain of BRCA2, also serves to regulate homologous recombination activity. Here we were interested in testing the role of the putative U. maydis BCCIP ortholog Bcp1 in DNA repair and recombination. In keeping with the mammalian paradigm, Bcp1 bound to the C-terminal region of Brh2. Mutants deleted of the gene were extremely slow growing, showed a delay passing through S phase and exhibited sensitivity to hydroxyurea, but were other-wise normal in DNA repair and homologous recombination. In the absence of Bcp1 cells were unable to maintain the wild type morphology when challenged by a DNA replication stress. These results suggest that Bcp1 could be involved in coordinating morphogenetic events with DNA processing during replication.",
publisher = "Elsevier, Amsterdam",
journal = "DNA Repair",
title = "Ortholog of BRCA2-interacting protein BCCIP controls morphogenetic responses during DNA replication stress in Ustilago maydis",
pages = "1660-1651",
number = "11",
volume = "6",
doi = "10.1016/j.dnarep.2007.05.012"
}

Mao, N., Zhou, Q., Kojić, M., Perez-Martin, J.,& Holloman, W. K.. (2007). Ortholog of BRCA2-interacting protein BCCIP controls morphogenetic responses during DNA replication stress in Ustilago maydis. in DNA Repair
Elsevier, Amsterdam., 6(11), 1651-1660.
https://doi.org/10.1016/j.dnarep.2007.05.012

Mao N, Zhou Q, Kojić M, Perez-Martin J, Holloman WK. Ortholog of BRCA2-interacting protein BCCIP controls morphogenetic responses during DNA replication stress in Ustilago maydis. in DNA Repair. 2007;6(11):1651-1660.
doi:10.1016/j.dnarep.2007.05.012 .

Mao, Ninghui, Zhou, Qingwen, Kojić, Milorad, Perez-Martin, Jose, Holloman, William K., "Ortholog of BRCA2-interacting protein BCCIP controls morphogenetic responses during DNA replication stress in Ustilago maydis" in DNA Repair, 6, no. 11 (2007):1651-1660,
https://doi.org/10.1016/j.dnarep.2007.05.012 . .

TY  - JOUR
AU  - Zhou, Qingwen
AU  - Kojić, Milorad
AU  - Cao, Zhimin
AU  - Lisby, Michael
AU  - Mazloum, Nayef A.
AU  - Holloman, William K.
PY  - 2007
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/284
AB  - Brh2, the BRCA2 ortholog in Ustilago maydis, enables recombinational repair of DNA by controlling Rad51 and is in turn regulated by Dss1. Interplay with Rad51. is conducted via the BRC element located in the N-terminal region of the protein and through an unrelated domain, CRE, at the C terminus. Mutation in either BRC or CRE severely reduces functional activity, but repair deficiency of the brh2 mutant can be complemented by expressing BRC and CRE on different molecules. This intermolecular complementation is dependent upon the presence of Dss1. Brh2 molecules associate through the region overlapping with the Dss1-interacting domain to form at least dimer-sized complexes, which in turn, can be dissociated by Dss1 to monomer. We propose that cooperation between BRC and CRE domains and the Dss1-provoked dissociation of Brh2 complexes are requisite features of Brh2's molecular mechanism.
PB  - Amer Soc Microbiology, Washington
T2  - Molecular and Cellular Biology
T1  - Dss1 interaction with Brh2 as a regulatory mechanism for recombinational repair
EP  - 2526
IS  - 7
SP  - 2512
VL  - 27
DO  - 10.1128/MCB.01907-06
ER  - 

@article{
author = "Zhou, Qingwen and Kojić, Milorad and Cao, Zhimin and Lisby, Michael and Mazloum, Nayef A. and Holloman, William K.",
year = "2007",
abstract = "Brh2, the BRCA2 ortholog in Ustilago maydis, enables recombinational repair of DNA by controlling Rad51 and is in turn regulated by Dss1. Interplay with Rad51. is conducted via the BRC element located in the N-terminal region of the protein and through an unrelated domain, CRE, at the C terminus. Mutation in either BRC or CRE severely reduces functional activity, but repair deficiency of the brh2 mutant can be complemented by expressing BRC and CRE on different molecules. This intermolecular complementation is dependent upon the presence of Dss1. Brh2 molecules associate through the region overlapping with the Dss1-interacting domain to form at least dimer-sized complexes, which in turn, can be dissociated by Dss1 to monomer. We propose that cooperation between BRC and CRE domains and the Dss1-provoked dissociation of Brh2 complexes are requisite features of Brh2's molecular mechanism.",
publisher = "Amer Soc Microbiology, Washington",
journal = "Molecular and Cellular Biology",
title = "Dss1 interaction with Brh2 as a regulatory mechanism for recombinational repair",
pages = "2526-2512",
number = "7",
volume = "27",
doi = "10.1128/MCB.01907-06"
}

Zhou, Q., Kojić, M., Cao, Z., Lisby, M., Mazloum, N. A.,& Holloman, W. K.. (2007). Dss1 interaction with Brh2 as a regulatory mechanism for recombinational repair. in Molecular and Cellular Biology
Amer Soc Microbiology, Washington., 27(7), 2512-2526.
https://doi.org/10.1128/MCB.01907-06

Zhou Q, Kojić M, Cao Z, Lisby M, Mazloum NA, Holloman WK. Dss1 interaction with Brh2 as a regulatory mechanism for recombinational repair. in Molecular and Cellular Biology. 2007;27(7):2512-2526.
doi:10.1128/MCB.01907-06 .

Zhou, Qingwen, Kojić, Milorad, Cao, Zhimin, Lisby, Michael, Mazloum, Nayef A., Holloman, William K., "Dss1 interaction with Brh2 as a regulatory mechanism for recombinational repair" in Molecular and Cellular Biology, 27, no. 7 (2007):2512-2526,
https://doi.org/10.1128/MCB.01907-06 . .

TY  - JOUR
AU  - Mao, Ninghui
AU  - Zhou, Qingwen
AU  - Kojić, Milorad
AU  - Perez-Martin, Jose
AU  - Holloman, William K.
PY  - 2007
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/278
AB  - The BRCA2 tumor suppressor functions in repair of DNA by homologous recombination through regulating the action of Rad51. In turn, BRCA2 appears to be regulated by other interacting proteins. Dss1, a small interacting protein that binds to the C-terminal domain, has a profound effect on activity as deduced from studies on the BRCA2-related protein Brh2 in Ustilago maydis. Evidence accumulating in mammalian systems suggests that BCCIP, another small interacting protein that binds to the C-terminal domain of BRCA2, also serves to regulate homologous recombination activity. Here we were interested in testing the role of the putative U. maydis BCCIP ortholog Bcp1 in DNA repair and recombination. In keeping with the mammalian paradigm, Bcp1 bound to the C-terminal region of Brh2. Mutants deleted of the gene were extremely slow growing, showed a delay passing through S phase and exhibited sensitivity to hydroxyurea, but were other-wise normal in DNA repair and homologous recombination. In the absence of Bcp1 cells were unable to maintain the wild type morphology when challenged by a DNA replication stress. These results suggest that Bcp1 could be involved in coordinating morphogenetic events with DNA processing during replication.
PB  - Elsevier, Amsterdam
T2  - DNA Repair
T1  - Ortholog of BRCA2-interacting protein BCCIP controls morphogenetic responses during DNA replication stress in Ustilago maydis
EP  - 1660
IS  - 11
SP  - 1651
VL  - 6
DO  - 10.1016/j.dnarep.2007.05.012
ER  - 

@article{
author = "Mao, Ninghui and Zhou, Qingwen and Kojić, Milorad and Perez-Martin, Jose and Holloman, William K.",
year = "2007",
abstract = "The BRCA2 tumor suppressor functions in repair of DNA by homologous recombination through regulating the action of Rad51. In turn, BRCA2 appears to be regulated by other interacting proteins. Dss1, a small interacting protein that binds to the C-terminal domain, has a profound effect on activity as deduced from studies on the BRCA2-related protein Brh2 in Ustilago maydis. Evidence accumulating in mammalian systems suggests that BCCIP, another small interacting protein that binds to the C-terminal domain of BRCA2, also serves to regulate homologous recombination activity. Here we were interested in testing the role of the putative U. maydis BCCIP ortholog Bcp1 in DNA repair and recombination. In keeping with the mammalian paradigm, Bcp1 bound to the C-terminal region of Brh2. Mutants deleted of the gene were extremely slow growing, showed a delay passing through S phase and exhibited sensitivity to hydroxyurea, but were other-wise normal in DNA repair and homologous recombination. In the absence of Bcp1 cells were unable to maintain the wild type morphology when challenged by a DNA replication stress. These results suggest that Bcp1 could be involved in coordinating morphogenetic events with DNA processing during replication.",
publisher = "Elsevier, Amsterdam",
journal = "DNA Repair",
title = "Ortholog of BRCA2-interacting protein BCCIP controls morphogenetic responses during DNA replication stress in Ustilago maydis",
pages = "1660-1651",
number = "11",
volume = "6",
doi = "10.1016/j.dnarep.2007.05.012"
}

Mao, N., Zhou, Q., Kojić, M., Perez-Martin, J.,& Holloman, W. K.. (2007). Ortholog of BRCA2-interacting protein BCCIP controls morphogenetic responses during DNA replication stress in Ustilago maydis. in DNA Repair
Elsevier, Amsterdam., 6(11), 1651-1660.
https://doi.org/10.1016/j.dnarep.2007.05.012

Mao N, Zhou Q, Kojić M, Perez-Martin J, Holloman WK. Ortholog of BRCA2-interacting protein BCCIP controls morphogenetic responses during DNA replication stress in Ustilago maydis. in DNA Repair. 2007;6(11):1651-1660.
doi:10.1016/j.dnarep.2007.05.012 .

Mao, Ninghui, Zhou, Qingwen, Kojić, Milorad, Perez-Martin, Jose, Holloman, William K., "Ortholog of BRCA2-interacting protein BCCIP controls morphogenetic responses during DNA replication stress in Ustilago maydis" in DNA Repair, 6, no. 11 (2007):1651-1660,
https://doi.org/10.1016/j.dnarep.2007.05.012 . .