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@article{1168310,
author = {Burgess, Rebecca C. and Šebesta, Marek and Sisáková, Alexandra and Marini Palomeque, María Victoria and Lisby, Michael and Damborský, Jiří and Klein, Hannah and Rothstein, Rodney and Krejčí, Lumír},
article_location = {SAN FRANCISCO},
article_number = {12},
doi = {http://dx.doi.org/10.1371/journal.pone.0082630},
keywords = {HOMOLOGOUS RECOMBINATION; SACCHAROMYCES-CEREVISIAE; POLYMERASE-DELTA; NUCLEOPROTEIN FILAMENT; REMODELING ENZYME; YEAST RAD51; SRS2; REPLICATION; CHROMATIN; ROLES},
language = {eng},
issn = {1932-6203},
journal = {Plos One},
title = {The PCNA Interaction Protein Box Sequence in Rad54 Is an Integral Part of Its ATPase Domain and Is Required for Efficient DNA Repair and Recombination},
volume = {8},
year = {2013}
}
TY - JOUR
ID - 1168310
AU - Burgess, Rebecca C. - Šebesta, Marek - Sisáková, Alexandra - Marini Palomeque, María Victoria - Lisby, Michael - Damborský, Jiří - Klein, Hannah - Rothstein, Rodney - Krejčí, Lumír
PY - 2013
TI - The PCNA Interaction Protein Box Sequence in Rad54 Is an Integral Part of Its ATPase Domain and Is Required for Efficient DNA Repair and Recombination
JF - Plos One
VL - 8
IS - 12
SP - "e82630"
EP - "e82630"
PB - PUBLIC LIBRARY SCIENCE
SN - 19326203
KW - HOMOLOGOUS RECOMBINATION
KW - SACCHAROMYCES-CEREVISIAE
KW - POLYMERASE-DELTA
KW - NUCLEOPROTEIN FILAMENT
KW - REMODELING ENZYME
KW - YEAST RAD51
KW - SRS2
KW - REPLICATION
KW - CHROMATIN
KW - ROLES
N2 - Rad54 is an ATP-driven translocase involved in the genome maintenance pathway of homologous recombination (HR) Although its activity has been implicated in several steps of HR, its exact role(s) at each step are still not fully understood. We have identified a new interaction between Rad54 and the replicative DNA clamp, proliferating cell nuclear antigen (PCNA). This interaction was only mildly weakened by the mutation of two key hydrophobic residues in the highly-conserved PCNA interaction PIP-box) of Rad54 (Rad54-AA). Intriguingly, the rad54-AA mutant cells displayed sensitivity to DNA damage and showed HR defects similar to the null mutant, despite retaining its ability to interact with HR proteins and to be recruited to HR foci in vivo. We therefore surmised that the PCNA interaction might be impaired in vivo and was Linable to promote repair synthesis during Indeed, the Rad54-AA mutant was defective in primer extension at the MAT locus as well as in vitro, but additional biochemical chemical analysis revealed that this mutant also had diminished ATPase activity and an inability to promote D-loop formation. Further mutational analysis of the putative PIP-box uncovered that other phenotypically relevant mutants in this domain also resulted in a loss of ATPase activity. Therefore, we have found that although Rad54 interacts with, the PIP-box motif likely plays only a minor role in stabilizing the PCNA interaction, and rather, this conserved domain is probably an extension of the ATPase domain III.
ER -
BURGESS, Rebecca C., Marek ŠEBESTA, Alexandra SISÁKOVÁ, María Victoria MARINI PALOMEQUE, Michael LISBY, Jiří DAMBORSKÝ, Hannah KLEIN, Rodney ROTHSTEIN and Lumír KREJČÍ. The PCNA Interaction Protein Box Sequence in Rad54 Is an Integral Part of Its ATPase Domain and Is Required for Efficient DNA Repair and Recombination. \textit{Plos One}. SAN FRANCISCO: PUBLIC LIBRARY SCIENCE, 2013, vol.~8, No~12, p.~''e82630'', 10 pp. ISSN~1932-6203. Available from: https://dx.doi.org/10.1371/journal.pone.0082630.
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