Role of ATP hydrolysis in the antirecombinase function of
Saccharomyces cerevisiae Srs2 protein.

J 2004

Role of ATP hydrolysis in the antirecombinase function of Saccharomyces cerevisiae Srs2 protein.

KREJČÍ, Lumír, Margaret MACRIS, Stephen VAN KOMEN, Jane VILLEMAIN, Tom ELLENBERGER et. al.

Basic information

Original name

Role of ATP hydrolysis in the antirecombinase function of Saccharomyces cerevisiae Srs2 protein.

Name in Czech

Úloha ATP hydrolýz pro anti-rekombinační aktivitu proteinu Srs2

Authors

KREJČÍ, Lumír (203 Czech Republic, guarantor), Margaret MACRIS (840 United States of America), Stephen VAN KOMEN (840 United States of America), Jane VILLEMAIN (840 United States of America), Tom ELLENBERGER (840 United States of America), Hannah KLEIN (840 United States of America) and Patrick SUNG (840 United States of America)

Edition

Journal of Biological Chemistry, Bethesda, USA, Amer. Soc. Biochem. Mol. Biol. 2004, 0021-9258

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10600 1.6 Biological sciences

Country of publisher

United States of America

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

URL

Impact factor

Impact factor: 6.355

Organization unit

Faculty of Medicine

UT WoS

000221570900050

Keywords in English

helicase; ATPase; Srs2; recombination; repair

Abstract

ORIG CZ

V originále

Mutants of the Saccharomyces cerevisiae SRS2 gene are hyperrecombinogenic and sensitive to genotoxic agents, and they exhibit a synthetic lethality with mutations that compromise DNA repair or other chromosomal processes. In addition, srs2 mutants fail to adapt or recover from DNA damage checkpoint-imposed G2/M arrest. These phenotypic consequences of ablating SRS2 function are effectively overcome by deleting genes of the RAD52 epistasis group that promote homologous recombination, implicating an untimely recombination as the underlying cause of the srs2 mutant phenotypes. TheSRS2-encodedproteinhasasingle-stranded (ss) DNA-dependent ATPase activity, a DNA helicase activity, and an ability to disassemble the Rad51-ssDNA nucleoprotein filament, which is the key catalytic intermediate in Rad51-mediated recombination reactions. To address the role of ATP hydrolysis in Srs2 protein function, we have constructed two mutant variants that are altered in the Walker type A sequence involved in the binding and hydrolysis of ATP. The srs2 K41A and srs2 K41R mutant proteins are both devoid of ATPase and helicase activities and the ability to displace Rad51 from ssDNA. Accordingly, yeast strains harboring these srs2 mutations are hyperrecombinogenic and sensitive to methylmethane sulfonate, and they become inviable upon introducing either the sgs1Delta or rad54Delta mutation. These results highlight the importance of the ATP hydrolysisfueled DNA motor activity in SRS2 functions.

In Czech

Vliv ATP na aktivitu Srs2

Citovat

KREJČÍ, Lumír, Margaret MACRIS, Stephen VAN KOMEN, Jane VILLEMAIN, Tom ELLENBERGER, Hannah KLEIN and Patrick SUNG. Role of ATP hydrolysis in the antirecombinase function of Saccharomyces cerevisiae Srs2 protein. Journal of Biological Chemistry. Bethesda, USA: Amer. Soc. Biochem. Mol. Biol., 2004, vol. 279, No 22, p. 23193-9, 6 pp. ISSN 0021-9258.

@article{708603,
   author = {Krejčí, Lumír and Macris, Margaret and Van Komen, Stephen and Villemain, Jane and Ellenberger, Tom and Klein, Hannah and Sung, Patrick},
   article_location = {Bethesda, USA},
   article_number = {22},
   keywords = {helicase; ATPase; Srs2; recombination; repair},
   language = {eng},
   issn = {0021-9258},
   journal = {Journal of Biological Chemistry},
   title = {Role of ATP hydrolysis in the antirecombinase function of Saccharomyces cerevisiae Srs2 protein.},
   url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&dopt=AbstractPlus&list_uids=15047689&query_hl=20&itool=pubmed_docsum},
   volume = {279},
   year = {2004}
}

TY  - JOUR
ID  - 708603
AU  - Krejčí, Lumír - Macris, Margaret - Van Komen, Stephen - Villemain, Jane - Ellenberger, Tom - Klein, Hannah - Sung, Patrick
PY  - 2004
TI  - Role of ATP hydrolysis in the antirecombinase function of Saccharomyces cerevisiae Srs2 protein.
JF  - Journal of Biological Chemistry
VL  - 279
IS  - 22
SP  - 23193-9
EP  - 23193-9
PB  - Amer. Soc. Biochem. Mol. Biol.
SN  - 00219258
KW  - helicase
KW  - ATPase
KW  - Srs2
KW  - recombination
KW  - repair
UR  - http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&dopt=AbstractPlus&list_uids=15047689&query_hl=20&itool=pubmed_docsum
L2  - http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&dopt=AbstractPlus&list_uids=15047689&query_hl=20&itool=pubmed_docsum
N2  - Mutants of the Saccharomyces cerevisiae SRS2 gene are hyperrecombinogenic and sensitive to genotoxic agents, and they exhibit a synthetic lethality with mutations that compromise DNA repair or other chromosomal processes. In addition, srs2 mutants fail to adapt or recover from DNA damage checkpoint-imposed G2/M arrest. These phenotypic consequences of ablating SRS2 function are effectively overcome by deleting genes of the RAD52 epistasis group that promote homologous recombination, implicating an untimely recombination as the underlying cause of the srs2 mutant phenotypes. TheSRS2-encodedproteinhasasingle-stranded (ss) DNA-dependent ATPase activity, a DNA helicase activity, and an ability to disassemble the Rad51-ssDNA nucleoprotein filament, which is the key catalytic intermediate in Rad51-mediated recombination reactions. To address the role of ATP hydrolysis in Srs2 protein function, we have constructed two mutant variants that are altered in the Walker type A sequence involved in the binding and hydrolysis of ATP. The srs2 K41A and srs2 K41R mutant proteins are both devoid of ATPase and helicase activities and the ability to displace Rad51 from ssDNA. Accordingly, yeast strains harboring these srs2 mutations are hyperrecombinogenic and sensitive to methylmethane sulfonate, and they become inviable upon introducing either the sgs1Delta or rad54Delta mutation. These results highlight the importance of the ATP hydrolysisfueled DNA motor activity in SRS2 functions.
ER  -

KREJČÍ, Lumír, Margaret MACRIS, Stephen VAN KOMEN, Jane VILLEMAIN, Tom ELLENBERGER, Hannah KLEIN and Patrick SUNG. Role of ATP hydrolysis in the antirecombinase function of Saccharomyces cerevisiae Srs2 protein. \textit{Journal of Biological Chemistry}. Bethesda, USA: Amer. Soc. Biochem. Mol. Biol., 2004, vol.~279, No~22, p.~23193-9, 6 pp. ISSN~0021-9258.

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