Dss1 interaction with Brh2 as a regulatory mechanism for recombinational repair
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2007
Аутори
Zhou, QingwenKojić, Milorad
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Cao, Zhimin
Lisby, Michael
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Mazloum, Nayef A.
Holloman, William K.
Чланак у часопису (Објављена верзија)
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Метаподаци
Приказ свих података о документуАпстракт
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.
Извор:
Molecular and Cellular Biology, 2007, 27, 7, 2512-2526Издавач:
- Amer Soc Microbiology, Washington
DOI: 10.1128/MCB.01907-06
ISSN: 0270-7306
PubMed: 17261595
WoS: 000245410500009
Scopus: 2-s2.0-34147195807
Институција/група
Institut za molekularnu genetiku i genetičko inženjerstvoTY - 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 . .