Dss1 Release Activates DNA Binding Potential in Brh2
Само за регистроване кориснике
2012
Чланак у часопису (Објављена верзија)
Метаподаци
Приказ свих података о документуАпстракт
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 Br...h2 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.
Извор:
Biochemistry, 2012, 51, 45, 9137-9146Издавач:
- Amer Chemical Soc, Washington
Финансирање / пројекти:
- National Institutes of Health [GM42482, GM79859]
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM079859, R01GM042482] Funding Source: NIH RePORTER
DOI: 10.1021/bi3011187
ISSN: 0006-2960
PubMed: 23094644
WoS: 000311189900012
Scopus: 2-s2.0-84869052477
Институција/група
Institut za molekularnu genetiku i genetičko inženjerstvoTY - 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 . .