DNA-binding Domain within the Brh2 N Terminus Is the Primary Interaction Site for Association with DNA
Апстракт
The C-terminal region of Brh2 (Brh2(CT)), the BRCA2 homolog in Ustilago maydis, is highly conserved and aligns with the DSS1/DNA-binding domain (DBD) of mammalian BRCA2, while the N-terminal region (Brh2(NT)) is poorly conserved and has no obvious functional domain except for the single Rad51-interacting BRC element. Paradoxically, Brh2(NT), but not Brh2(CT), complements the DNA repair and recombination deficiency of the brh2 mutant. We show here that Brh2(NT) exhibits an unexpected DNA binding activity with properties similar to that of the full-length protein. Deletion mapping localized the region responsible for the DNA binding activity to a stretch of residues between the BRC element and the canonical DBD. A heterologous DNA-binding domain from the large subunit of replication protein A substituted for the endogenous binding region within Brh2(NT) in supporting DNA repair. Rad51-promoted strand invasion was stimulated by Brh2(NT), but required the presence of the BRC element. The f...indings suggest a model in which Brh2(NT) serves as the principal site for association with DNA, while the Brh2(CT) provides a means for regulation.
Извор:
Journal of Biological Chemistry, 2009, 284, 13, 8265-8273Издавач:
- Amer Soc Biochemistry Molecular Biology Inc, Bethesda
Финансирање / пројекти:
- National Institutes of Health [GM42482, GM79859]
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM079859, R01GM042482] Funding Source: NIH RePORTER
DOI: 10.1074/jbc.M809226200
ISSN: 0021-9258
PubMed: 19182269
WoS: 000264397800010
Scopus: 2-s2.0-67649821713
Институција/група
Institut za molekularnu genetiku i genetičko inženjerstvoTY - JOUR AU - Zhou, Qingwen AU - Kojić, Milorad AU - Holloman, William K. PY - 2009 UR - https://imagine.imgge.bg.ac.rs/handle/123456789/360 AB - The C-terminal region of Brh2 (Brh2(CT)), the BRCA2 homolog in Ustilago maydis, is highly conserved and aligns with the DSS1/DNA-binding domain (DBD) of mammalian BRCA2, while the N-terminal region (Brh2(NT)) is poorly conserved and has no obvious functional domain except for the single Rad51-interacting BRC element. Paradoxically, Brh2(NT), but not Brh2(CT), complements the DNA repair and recombination deficiency of the brh2 mutant. We show here that Brh2(NT) exhibits an unexpected DNA binding activity with properties similar to that of the full-length protein. Deletion mapping localized the region responsible for the DNA binding activity to a stretch of residues between the BRC element and the canonical DBD. A heterologous DNA-binding domain from the large subunit of replication protein A substituted for the endogenous binding region within Brh2(NT) in supporting DNA repair. Rad51-promoted strand invasion was stimulated by Brh2(NT), but required the presence of the BRC element. The findings suggest a model in which Brh2(NT) serves as the principal site for association with DNA, while the Brh2(CT) provides a means for regulation. PB - Amer Soc Biochemistry Molecular Biology Inc, Bethesda T2 - Journal of Biological Chemistry T1 - DNA-binding Domain within the Brh2 N Terminus Is the Primary Interaction Site for Association with DNA EP - 8273 IS - 13 SP - 8265 VL - 284 DO - 10.1074/jbc.M809226200 ER -
@article{ author = "Zhou, Qingwen and Kojić, Milorad and Holloman, William K.", year = "2009", abstract = "The C-terminal region of Brh2 (Brh2(CT)), the BRCA2 homolog in Ustilago maydis, is highly conserved and aligns with the DSS1/DNA-binding domain (DBD) of mammalian BRCA2, while the N-terminal region (Brh2(NT)) is poorly conserved and has no obvious functional domain except for the single Rad51-interacting BRC element. Paradoxically, Brh2(NT), but not Brh2(CT), complements the DNA repair and recombination deficiency of the brh2 mutant. We show here that Brh2(NT) exhibits an unexpected DNA binding activity with properties similar to that of the full-length protein. Deletion mapping localized the region responsible for the DNA binding activity to a stretch of residues between the BRC element and the canonical DBD. A heterologous DNA-binding domain from the large subunit of replication protein A substituted for the endogenous binding region within Brh2(NT) in supporting DNA repair. Rad51-promoted strand invasion was stimulated by Brh2(NT), but required the presence of the BRC element. The findings suggest a model in which Brh2(NT) serves as the principal site for association with DNA, while the Brh2(CT) provides a means for regulation.", publisher = "Amer Soc Biochemistry Molecular Biology Inc, Bethesda", journal = "Journal of Biological Chemistry", title = "DNA-binding Domain within the Brh2 N Terminus Is the Primary Interaction Site for Association with DNA", pages = "8273-8265", number = "13", volume = "284", doi = "10.1074/jbc.M809226200" }
Zhou, Q., Kojić, M.,& Holloman, W. K.. (2009). DNA-binding Domain within the Brh2 N Terminus Is the Primary Interaction Site for Association with DNA. in Journal of Biological Chemistry Amer Soc Biochemistry Molecular Biology Inc, Bethesda., 284(13), 8265-8273. https://doi.org/10.1074/jbc.M809226200
Zhou Q, Kojić M, Holloman WK. DNA-binding Domain within the Brh2 N Terminus Is the Primary Interaction Site for Association with DNA. in Journal of Biological Chemistry. 2009;284(13):8265-8273. doi:10.1074/jbc.M809226200 .
Zhou, Qingwen, Kojić, Milorad, Holloman, William K., "DNA-binding Domain within the Brh2 N Terminus Is the Primary Interaction Site for Association with DNA" in Journal of Biological Chemistry, 284, no. 13 (2009):8265-8273, https://doi.org/10.1074/jbc.M809226200 . .