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Molecular anatomy of the recombination mediator function of Saccharomyces cerevisiae Rad52.
J Biol Chem. 2008 May 02; 283(18):12166-74.JB

Abstract

A helical filament of Rad51 on single-strand DNA (ssDNA), called the presynaptic filament, catalyzes DNA joint formation during homologous recombination. Rad52 facilitates presynaptic filament assembly, and this recombination mediator activity is thought to rely on the interactions of Rad52 with Rad51, the ssDNA-binding protein RPA, and ssDNA. The N-terminal region of Rad52, which has DNA binding activity and an oligomeric structure, is thought to be crucial for mediator activity and recombination. Unexpectedly, we find that the C-terminal region of Rad52 also harbors a DNA binding function. Importantly, the Rad52 C-terminal portion alone can promote Rad51 presynaptic filament assembly. The middle portion of Rad52 associates with DNA-bound RPA and contributes to the recombination mediator activity. Accordingly, expression of a protein species that harbors the middle and C-terminal regions of Rad52 in the rad52 Delta327 background enhances the association of Rad51 protein with a HO-made DNA double-strand break and partially complements the methylmethane sulfonate sensitivity of the mutant cells. Our results provide a mechanistic framework for rationalizing the multi-faceted role of Rad52 in recombination and DNA repair.

Authors+Show Affiliations

Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven, Connecticut 06520, USA.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

18310075

Citation

Seong, Changhyun, et al. "Molecular Anatomy of the Recombination Mediator Function of Saccharomyces Cerevisiae Rad52." The Journal of Biological Chemistry, vol. 283, no. 18, 2008, pp. 12166-74.
Seong C, Sehorn MG, Plate I, et al. Molecular anatomy of the recombination mediator function of Saccharomyces cerevisiae Rad52. J Biol Chem. 2008;283(18):12166-74.
Seong, C., Sehorn, M. G., Plate, I., Shi, I., Song, B., Chi, P., Mortensen, U., Sung, P., & Krejci, L. (2008). Molecular anatomy of the recombination mediator function of Saccharomyces cerevisiae Rad52. The Journal of Biological Chemistry, 283(18), 12166-74. https://doi.org/10.1074/jbc.M800763200
Seong C, et al. Molecular Anatomy of the Recombination Mediator Function of Saccharomyces Cerevisiae Rad52. J Biol Chem. 2008 May 2;283(18):12166-74. PubMed PMID: 18310075.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Molecular anatomy of the recombination mediator function of Saccharomyces cerevisiae Rad52. AU - Seong,Changhyun, AU - Sehorn,Michael G, AU - Plate,Iben, AU - Shi,Idina, AU - Song,Binwei, AU - Chi,Peter, AU - Mortensen,Uffe, AU - Sung,Patrick, AU - Krejci,Lumir, Y1 - 2008/02/29/ PY - 2008/3/4/pubmed PY - 2008/6/20/medline PY - 2008/3/4/entrez SP - 12166 EP - 74 JF - The Journal of biological chemistry JO - J Biol Chem VL - 283 IS - 18 N2 - A helical filament of Rad51 on single-strand DNA (ssDNA), called the presynaptic filament, catalyzes DNA joint formation during homologous recombination. Rad52 facilitates presynaptic filament assembly, and this recombination mediator activity is thought to rely on the interactions of Rad52 with Rad51, the ssDNA-binding protein RPA, and ssDNA. The N-terminal region of Rad52, which has DNA binding activity and an oligomeric structure, is thought to be crucial for mediator activity and recombination. Unexpectedly, we find that the C-terminal region of Rad52 also harbors a DNA binding function. Importantly, the Rad52 C-terminal portion alone can promote Rad51 presynaptic filament assembly. The middle portion of Rad52 associates with DNA-bound RPA and contributes to the recombination mediator activity. Accordingly, expression of a protein species that harbors the middle and C-terminal regions of Rad52 in the rad52 Delta327 background enhances the association of Rad51 protein with a HO-made DNA double-strand break and partially complements the methylmethane sulfonate sensitivity of the mutant cells. Our results provide a mechanistic framework for rationalizing the multi-faceted role of Rad52 in recombination and DNA repair. SN - 0021-9258 UR - https://www.unboundmedicine.com/medline/citation/18310075/Molecular_anatomy_of_the_recombination_mediator_function_of_Saccharomyces_cerevisiae_Rad52_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0021-9258(20)49319-6 DB - PRIME DP - Unbound Medicine ER -