Detailed Information on Publication Record
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
Tags
International impact, Reviewed
Změněno: 15/5/2009 22:54, doc. Mgr. Lumír Krejčí, Ph.D.
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