Dss1 Regulates Interaction of Brh2 with DNA
Само за регистроване кориснике
2009
Чланак у часопису (Објављена верзија)
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Метаподаци
Приказ свих података о документуАпстракт
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.
Извор:
Biochemistry, 2009, 48, 50, 11929-11938Издавач:
- Amer Chemical Soc, Washington
Финансирање / пројекти:
- National Institutes of Health [GM42482, GM79859]
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM042482, R01GM079859] Funding Source: NIH RePORTER
DOI: 10.1021/bi901775j
ISSN: 0006-2960
PubMed: 19919104
WoS: 000272645400013
Scopus: 2-s2.0-72449145252
Институција/група
Institut za molekularnu genetiku i genetičko inženjerstvoTY - 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 . .