Brh2-dss1 interplay enables properly controlled recombination in Ustilago maydis
Apstrakt
Brh2, the BRCA2 homolog in Ustilago maydis, functions in recombinational repair of DNA damage by regulating Rad51 and is, in turn, regulated by Dss1. Dss1 is not required for Brh2 stability in vivo, nor for Brh2 to associate with Rad51, but is required for formation of green fluorescent protein (GFP)-Rad51 foci following DNA damage by gamma radiation. To understand more about the interplay between Brh2 and Dss1, we isolated mutant variants of Brh2 able to bypass the requirement for Dss1. These variants were found to lack the entire C-terminal DNA-Dss1 binding domain but to maintain the N-terminal region harboring the Rad51-interacting BRC element. GFP-Rad51 focus formation was nearly normal in brh2 mutant cells expressing a representative Brh2 variant with the C-terminal domain deleted. These findings suggest that the N-terminal region of Brh2 has an innate ability to organize Rad51. Survival after DNA damage was almost fully restored by a chimeric form of Brh2 having a DNA-binding dom...ain from RPA70 fused to the Brh2 N-terminal domain, but Rad51 focus formation and mitotic recombination were elevated above wild-type levels. The results provide evidence for a mechanism in which Dss1 activates a Brh2-Rad51 complex and balances a finely regulated recombinational repair system.
Izvor:
Molecular and Cellular Biology, 2005, 25, 7, 2547-2557Izdavač:
- Amer Soc Microbiology, Washington
Finansiranje / projekti:
- NIGMS NIH HHS [R01 GM042482, GM42482] Funding Source: Medline
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM042482] Funding Source: NIH RePORTER
DOI: 10.1128/MCB.25.7.2547-2557.2005
ISSN: 0270-7306
PubMed: 15767662
WoS: 000227679000003
Scopus: 2-s2.0-15044340651
Institucija/grupa
Institut za molekularnu genetiku i genetičko inženjerstvoTY - JOUR AU - Kojić, Milorad AU - Zhou, QW AU - Lisby, M AU - Holloman, WK PY - 2005 UR - https://imagine.imgge.bg.ac.rs/handle/123456789/235 AB - Brh2, the BRCA2 homolog in Ustilago maydis, functions in recombinational repair of DNA damage by regulating Rad51 and is, in turn, regulated by Dss1. Dss1 is not required for Brh2 stability in vivo, nor for Brh2 to associate with Rad51, but is required for formation of green fluorescent protein (GFP)-Rad51 foci following DNA damage by gamma radiation. To understand more about the interplay between Brh2 and Dss1, we isolated mutant variants of Brh2 able to bypass the requirement for Dss1. These variants were found to lack the entire C-terminal DNA-Dss1 binding domain but to maintain the N-terminal region harboring the Rad51-interacting BRC element. GFP-Rad51 focus formation was nearly normal in brh2 mutant cells expressing a representative Brh2 variant with the C-terminal domain deleted. These findings suggest that the N-terminal region of Brh2 has an innate ability to organize Rad51. Survival after DNA damage was almost fully restored by a chimeric form of Brh2 having a DNA-binding domain from RPA70 fused to the Brh2 N-terminal domain, but Rad51 focus formation and mitotic recombination were elevated above wild-type levels. The results provide evidence for a mechanism in which Dss1 activates a Brh2-Rad51 complex and balances a finely regulated recombinational repair system. PB - Amer Soc Microbiology, Washington T2 - Molecular and Cellular Biology T1 - Brh2-dss1 interplay enables properly controlled recombination in Ustilago maydis EP - 2557 IS - 7 SP - 2547 VL - 25 DO - 10.1128/MCB.25.7.2547-2557.2005 ER -
@article{ author = "Kojić, Milorad and Zhou, QW and Lisby, M and Holloman, WK", year = "2005", abstract = "Brh2, the BRCA2 homolog in Ustilago maydis, functions in recombinational repair of DNA damage by regulating Rad51 and is, in turn, regulated by Dss1. Dss1 is not required for Brh2 stability in vivo, nor for Brh2 to associate with Rad51, but is required for formation of green fluorescent protein (GFP)-Rad51 foci following DNA damage by gamma radiation. To understand more about the interplay between Brh2 and Dss1, we isolated mutant variants of Brh2 able to bypass the requirement for Dss1. These variants were found to lack the entire C-terminal DNA-Dss1 binding domain but to maintain the N-terminal region harboring the Rad51-interacting BRC element. GFP-Rad51 focus formation was nearly normal in brh2 mutant cells expressing a representative Brh2 variant with the C-terminal domain deleted. These findings suggest that the N-terminal region of Brh2 has an innate ability to organize Rad51. Survival after DNA damage was almost fully restored by a chimeric form of Brh2 having a DNA-binding domain from RPA70 fused to the Brh2 N-terminal domain, but Rad51 focus formation and mitotic recombination were elevated above wild-type levels. The results provide evidence for a mechanism in which Dss1 activates a Brh2-Rad51 complex and balances a finely regulated recombinational repair system.", publisher = "Amer Soc Microbiology, Washington", journal = "Molecular and Cellular Biology", title = "Brh2-dss1 interplay enables properly controlled recombination in Ustilago maydis", pages = "2557-2547", number = "7", volume = "25", doi = "10.1128/MCB.25.7.2547-2557.2005" }
Kojić, M., Zhou, Q., Lisby, M.,& Holloman, W.. (2005). Brh2-dss1 interplay enables properly controlled recombination in Ustilago maydis. in Molecular and Cellular Biology Amer Soc Microbiology, Washington., 25(7), 2547-2557. https://doi.org/10.1128/MCB.25.7.2547-2557.2005
Kojić M, Zhou Q, Lisby M, Holloman W. Brh2-dss1 interplay enables properly controlled recombination in Ustilago maydis. in Molecular and Cellular Biology. 2005;25(7):2547-2557. doi:10.1128/MCB.25.7.2547-2557.2005 .
Kojić, Milorad, Zhou, QW, Lisby, M, Holloman, WK, "Brh2-dss1 interplay enables properly controlled recombination in Ustilago maydis" in Molecular and Cellular Biology, 25, no. 7 (2005):2547-2557, https://doi.org/10.1128/MCB.25.7.2547-2557.2005 . .