PRAKASH, Rohit, Lumír KREJČÍ, Stephen VAN KOMEN, Anke SCHURER, Wilfried KRAMER and Patrick SUNG. Saccharomyces cerevisiae MPH1 gene, required for homologous recombination-mediated mutation avoidance, encodes a 3' to 5' DNA helicase. Journal of Biological Chemistry. Bethesda, USA: Amer. Soc. Biochem. Mol. Biol., 2005, vol. 280, No 9, p. 7854-60, 6 pp. ISSN 0021-9258.
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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
Original 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
WWW URL
Impact factor Impact factor: 5.854
Organization unit Faculty of Science
UT WoS 000227395700052
Keywords in English Mph1; helicase; recombination; repair
Tags helicase, Mph1, recombination, repair
Tags International impact, Reviewed
Changed by Changed by: doc. Mgr. Lumír Krejčí, Ph.D., učo 18098. Changed: 15/5/2009 22:54.
Abstract
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.
Abstract (in Czech)
Charakterizace proteinu Mph1
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