Dss1 Release Activates DNA Binding Potential in Brh2
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 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.
Source:
Biochemistry, 2012, 51, 45, 9137-9146Publisher:
- Amer Chemical Soc, Washington
Funding / projects:
- 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
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Institution/Community
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 . .