J 2005

Saccharomyces cerevisiae MPH1 gene, required for homologous recombination-mediated mutation avoidance, encodes a 3' to 5' DNA helicase.

PRAKASH, Rohit, Lumír KREJČÍ, Stephen VAN KOMEN, Anke SCHURER, Wilfried KRAMER et. al.

Basic information

Original name

Saccharomyces cerevisiae MPH1 gene, required for homologous recombination-mediated mutation avoidance, encodes a 3' to 5' DNA helicase.

Name in Czech

Kvasinkový gen MPH1 je potřebný pro homologní rekombinaci

Authors

PRAKASH, Rohit (356 India), Lumír KREJČÍ (203 Czech Republic, guarantor), Stephen VAN KOMEN (840 United States of America), Anke SCHURER (276 Germany), Wilfried KRAMER (276 Germany) and Patrick SUNG (840 United States of America)

Edition

Journal of Biological Chemistry, Bethesda, USA, Amer. Soc. Biochem. Mol. Biol. 2005, 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:

Impact factor

Impact factor: 5.854

Organization unit

Faculty of Science

UT WoS

000227395700052

Keywords in English

Mph1; helicase; recombination; repair

Tags

International impact, Reviewed
Změněno: 15/5/2009 22:54, doc. Mgr. Lumír Krejčí, Ph.D.

Abstract

V originále

The MPH1 (mutator pHenotype 1) gene of Saccharomyces cerevisiae was identified on the basis of elevated spontaneous mutation rates of haploid cells deleted for this gene. Further studies showed that MPH1 functions to channel DNA lesions into an error-free DNA repair pathway. The Mph1 protein contains the seven conserved motifs of the superfamily 2 (SF2) family of nucleic acid unwinding enzymes. Genetic analyses have found epistasis of the mph1 deletion with mutations in the RAD52 gene group that mediates homologous recombination and DNA repair by homologous recombination. To begin dissecting the biochemical functions of the MPH1-encoded product, we have expressed it in yeast cells and purified it to near homogeneity. We show that Mph1 has a robust ATPase function that requires single-stranded DNA for activation. Consistent with its homology to members of the SF2 helicase family, we find a DNA helicase activity in Mph1. We present data to demonstrate that the Mph1 DNA helicase activity is fueled by ATP hydrolysis and has a 3' to 5' polarity with respect to the DNA strand on which this protein translocates. The DNA helicase activity of Mph1 is enhanced by the heterotrimeric single-stranded DNA binding protein replication protein A. These results, thus, establish Mph1 as an ATP-dependent DNA helicase, and the availability of purified Mph1 should facilitate efforts at deciphering the role of this protein in homologous recombination and mutation avoidance.

In Czech

Charakterizace proteinu Mph1