Detailed Information on Publication Record
2009
Co-operativity of Mus81-Mms4 with Rad54 in the resolution of recombination and replication intermediates.
MATULOVÁ, Petra, María Victoria MARINI PALOMEQUE, RC BURGESS, Alexandra SISÁKOVÁ, Youngho KWON et. al.Basic information
Original name
Co-operativity of Mus81-Mms4 with Rad54 in the resolution of recombination and replication intermediates.
Name in Czech
Stimulace Mus81/MMS4 endonukleázy Rad54 proteinem při rozpouštění rekombinačních a replikačních meziproduktů
Authors
MATULOVÁ, Petra (203 Czech Republic), María Victoria MARINI PALOMEQUE (858 Uruguay), RC BURGESS (840 United States of America), Alexandra SISÁKOVÁ (703 Slovakia), Youngho KWON (840 United States of America), Rodney ROTHSTEIN (840 United States of America), Patrick SUNG (840 United States of America) and Lumír KREJČÍ (203 Czech Republic, guarantor)
Edition
J Biol Chem. 2009, 1083-351X
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
Impact factor
Impact factor: 5.328
RIV identification code
RIV/00216224:14310/09:00029170
Organization unit
Faculty of Science
UT WoS
000264195600035
Keywords in English
repair; recombination; DSB; replication
Tags
Tags
International impact, Reviewed
Změněno: 1/7/2009 08:05, doc. Mgr. Lumír Krejčí, Ph.D.
V originále
The Saccharomyces cerevisiae Mus81-Mms4 protein complex, a DNA structure-specific endonuclease, helps preserve genomic integrity by resolving pathological DNA structures that arise from damaged or aborted replication forks and may also play a role in the resolution of DNA intermediates arising through homologous recombination. Previous yeast two-hybrid studies have found an interaction of the Mus81 protein with Rad54, a Swi2/Snf2-like factor that serves multiple roles in homologous recombination processes. However, the functional significance of this novel interaction remains unknown. Here, using highly purified S. cerevisiae proteins, we show that Rad54 strongly stimulates the Mus81-Mms4 nuclease activity on a broad range of DNA substrates. This nuclease enhancement does not require ATP binding nor its hydrolysis by Rad54. We present evidence that Rad54 acts by targeting Mus81-Mms4 complex to its DNA substrates. In addition, we demonstrate that the Rad54-mediated enhancement of the Mus81-Mms4-Eme1 nuclease function is evolutionarily conserved. We propose that Mus81-Mms4 together with Rad54 efficiently process perturbed replication forks to promote recovery and may constitute an alternative mechanism to the resolution/dissolution of the recombination intermediates by Sgs1-Top3. These findings provide functional insights into the biological importance of the higher order complex of Mus81-Mms4 or its orthologue with Rad54.
In Czech
Charakterizace vlivu proteinu Rad54 na nukleázovou aktivitu komplexu Mus81/Mms4.
Links
| GA301/09/1917, research and development project |
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| GD203/09/H046, research and development project |
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| LC06030, research and development project |
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| MSM0021622413, plan (intention) |
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