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Rad52 promotes second-end DNA capture in double-stranded break repair to form complement-stabilized joint molecules.
Proc Natl Acad Sci U S A. 2009 Mar 03; 106(9):3077-82.PN

Abstract

Saccharomyces cerevisiae Rad52 performs multiple functions during the recombinational repair of double-stranded DNA (dsDNA) breaks (DSBs). It mediates assembly of Rad51 onto single-stranded DNA (ssDNA) that is complexed with replication protein A (RPA); the resulting nucleoprotein filament pairs with homologous dsDNA to form joint molecules. Rad52 also catalyzes the annealing of complementary strands of ssDNA, even when they are complexed with RPA. Both Rad51 and Rad52 can be envisioned to promote "second-end capture," a step that pairs the ssDNA generated by processing of the second end of a DSB to the joint molecule formed by invasion of the target dsDNA by the first processed end. Here, we show that Rad52 promotes annealing of complementary ssDNA that is complexed with RPA to the displaced strand of a joint molecule, to form a complement-stabilized joint molecule. RecO, a prokaryotic homolog of Rad52, cannot form complement-stabilized joint molecules with RPA-ssDNA complexes, nor can Rad52 promote second-end capture when the ssDNA is bound with either human RPA or the prokaryotic ssDNA-binding protein, SSB, indicating a species-specific process. We conclude that Rad52 participates in second-end capture by annealing a resected DNA break, complexed with RPA, to the joint molecule product of single-end invasion event. These studies support a role for Rad52-promoted annealing in the formation of Holliday junctions in DSB repair.

Authors+Show Affiliations

Department of Microbiology, University of California, Davis, CA 95616-8665, USA.No 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

19204284

Citation

Nimonkar, Amitabh V., et al. "Rad52 Promotes Second-end DNA Capture in Double-stranded Break Repair to Form Complement-stabilized Joint Molecules." Proceedings of the National Academy of Sciences of the United States of America, vol. 106, no. 9, 2009, pp. 3077-82.
Nimonkar AV, Sica RA, Kowalczykowski SC. Rad52 promotes second-end DNA capture in double-stranded break repair to form complement-stabilized joint molecules. Proc Natl Acad Sci U S A. 2009;106(9):3077-82.
Nimonkar, A. V., Sica, R. A., & Kowalczykowski, S. C. (2009). Rad52 promotes second-end DNA capture in double-stranded break repair to form complement-stabilized joint molecules. Proceedings of the National Academy of Sciences of the United States of America, 106(9), 3077-82. https://doi.org/10.1073/pnas.0813247106
Nimonkar AV, Sica RA, Kowalczykowski SC. Rad52 Promotes Second-end DNA Capture in Double-stranded Break Repair to Form Complement-stabilized Joint Molecules. Proc Natl Acad Sci U S A. 2009 Mar 3;106(9):3077-82. PubMed PMID: 19204284.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Rad52 promotes second-end DNA capture in double-stranded break repair to form complement-stabilized joint molecules. AU - Nimonkar,Amitabh V, AU - Sica,R Alejandro, AU - Kowalczykowski,Stephen C, Y1 - 2009/02/09/ PY - 2009/2/11/entrez PY - 2009/2/11/pubmed PY - 2009/4/2/medline SP - 3077 EP - 82 JF - Proceedings of the National Academy of Sciences of the United States of America JO - Proc Natl Acad Sci U S A VL - 106 IS - 9 N2 - Saccharomyces cerevisiae Rad52 performs multiple functions during the recombinational repair of double-stranded DNA (dsDNA) breaks (DSBs). It mediates assembly of Rad51 onto single-stranded DNA (ssDNA) that is complexed with replication protein A (RPA); the resulting nucleoprotein filament pairs with homologous dsDNA to form joint molecules. Rad52 also catalyzes the annealing of complementary strands of ssDNA, even when they are complexed with RPA. Both Rad51 and Rad52 can be envisioned to promote "second-end capture," a step that pairs the ssDNA generated by processing of the second end of a DSB to the joint molecule formed by invasion of the target dsDNA by the first processed end. Here, we show that Rad52 promotes annealing of complementary ssDNA that is complexed with RPA to the displaced strand of a joint molecule, to form a complement-stabilized joint molecule. RecO, a prokaryotic homolog of Rad52, cannot form complement-stabilized joint molecules with RPA-ssDNA complexes, nor can Rad52 promote second-end capture when the ssDNA is bound with either human RPA or the prokaryotic ssDNA-binding protein, SSB, indicating a species-specific process. We conclude that Rad52 participates in second-end capture by annealing a resected DNA break, complexed with RPA, to the joint molecule product of single-end invasion event. These studies support a role for Rad52-promoted annealing in the formation of Holliday junctions in DSB repair. SN - 1091-6490 UR - https://www.unboundmedicine.com/medline/citation/19204284/Rad52_promotes_second_end_DNA_capture_in_double_stranded_break_repair_to_form_complement_stabilized_joint_molecules_ L2 - http://www.pnas.org/cgi/pmidlookup?view=long&pmid=19204284 DB - PRIME DP - Unbound Medicine ER -