Srs2 Disassembles Rad51 Filaments by a Protein-Protein Interaction Triggering ATP Turnover and Dissociation of Rad51 from DNA

ANTONY, Edwin; Eric J. TOMKO; Qi XIAO; Lumír KREJČÍ; Timothy M. LOHMAN and Tom ELLENBERGER. Srs2 Disassembles Rad51 Filaments by a Protein-Protein Interaction Triggering ATP Turnover and Dissociation of Rad51 from DNA. Molecular Cell. 2009, vol. 35, No 1, p. 105-115, 10 pp. ISSN 1097-2765.

Basic information

Original name

Srs2 Disassembles Rad51 Filaments by a Protein-Protein Interaction Triggering ATP Turnover and Dissociation of Rad51 from DNA

Name in Czech

Srs2 protein rozpouští Rad51 vlákna díky protein-protein interakčně spuštěné hydrolýze ATP

Authors

ANTONY, Edwin; Eric J. TOMKO; Qi XIAO; Lumír KREJČÍ; Timothy M. LOHMAN and Tom ELLENBERGER

Edition

Molecular Cell, 2009, 1097-2765

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Other information

Language

English

Type of outcome

Article in a journal

Field of Study

10600 1.6 Biological sciences

Country of publisher

United States of America

Confidentiality degree

is not subject to a state or trade secret

Impact factor

Impact factor: 14.608

Marked to be transferred to RIV

Yes

RIV identification code

RIV/00216224:14310/09:00029284

Organization unit

Faculty of Science

UT WoS

000268003300010

Keywords in English

DNA repair; DNA damage; replication; genomic instability

Tags

DNA damage, DNA repair, genomic instability, replication

Tags

International impact, Reviewed

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Abstract

In the original language

Rad51 is a DNA recombinase functioning in the repair of DNA double-strand breaks and the generation of genetic diversity by homologous recombination (HR). In the presence of ATP, Rad51 self-assembles into an extended polymer on single-stranded DNA to catalyze strand exchange. Inappropriate HR causes genomic instability and it is normally prevented by remodeling enzymes that antagonize the activities of Rad51 nucleoprotein filaments. In yeast, the Srs2 helicase/translocase suppresses HR by clearing Rad51 polymers from single-stranded DNA. We have examined the mechanism of disassembly of Rad51 nucleoprotein filaments by Srs2 and find that a physical interaction between Rad51 and the C-terminal region of Srs2 triggers ATP hydrolysis within the Rad51 filament, causing Rad51 to dissociate from DNA. This allosteric mechanism explains the biological specialization of Srs2 as a DNA motor protein that antagonizes HR.

In Czech

Charakterizace působení Srs2 proteinu na Rad51 nukleoproteinové vlákno

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Links

GA301/09/1917, research and development project	Name: Štěpení replikačních-rekombinačních DNA meziproduktů a jejich úloha při nestabilitě genomu Investor: Czech Science Foundation
GD203/09/H046, research and development project	Name: Biochemie na rozcestí mezi in silico a in vitro Investor: Czech Science Foundation
LC06030, research and development project	Name: Biomolekulární centrum Investor: Ministry of Education, Youth and Sports of the CR, Biomolecular centre
MSM0021622413, plan (intention)	Name: Proteiny v metabolismu a při interakci organismů s prostředím Investor: Ministry of Education, Youth and Sports of the CR, Proteins in metabolism and interaction of organisms with the environment