Active displacement of RecA filaments by UvrD translocase activity

The UvrD helicase has been implicated in the disassembly of RecA nucleoprotein filaments in vivo and in vitro. We demonstrate that UvrD utilizes an active mechanism to remove RecA from the DNA. Efficient RecA removal depends on the availability of DNA binding sites for UvrD and/or the accessibility...

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Main Authors:	Petrova, Vessela, Chen, Stefanie H., Molzberger, Eileen T., Tomko, Eric, Chitteni-Pattu, Sindhu, Jia, Haifeng, Ordabayev, Yerdos, Lohman, Timothy M., Cox, Michael M.
Format:	Online
Language:	English
Published:	Oxford University Press 2015
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4417151/

id	pubmed-4417151
recordtype	oai_dc
spelling	pubmed-44171512015-05-12 Active displacement of RecA filaments by UvrD translocase activity Petrova, Vessela Chen, Stefanie H. Molzberger, Eileen T. Tomko, Eric Chitteni-Pattu, Sindhu Jia, Haifeng Ordabayev, Yerdos Lohman, Timothy M. Cox, Michael M. Nucleic Acid Enzymes The UvrD helicase has been implicated in the disassembly of RecA nucleoprotein filaments in vivo and in vitro. We demonstrate that UvrD utilizes an active mechanism to remove RecA from the DNA. Efficient RecA removal depends on the availability of DNA binding sites for UvrD and/or the accessibility of the RecA filament ends. The removal of RecA from DNA also requires ATP hydrolysis by the UvrD helicase but not by RecA protein. The RecA-removal activity of UvrD is slowed by RecA variants with enhanced DNA-binding properties. The ATPase rate of UvrD during RecA removal is much slower than the ATPase activity of UvrD when it is functioning either as a translocase or a helicase on DNA in the absence of RecA. Thus, in this context UvrD may operate in a specialized disassembly mode. Oxford University Press 2015-04-30 2015-03-30 /pmc/articles/PMC4417151/ /pubmed/25824953 http://dx.doi.org/10.1093/nar/gkv186 Text en © The Author(s) 2015. Published by Oxford University Press on behalf of Nucleic Acids Research. http://creativecommons.org/licenses/by-nc/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com
repository_type	Open Access Journal
institution_category	Foreign Institution
institution	US National Center for Biotechnology Information
building	NCBI PubMed
collection	Online Access
language	English
format	Online
author	Petrova, Vessela Chen, Stefanie H. Molzberger, Eileen T. Tomko, Eric Chitteni-Pattu, Sindhu Jia, Haifeng Ordabayev, Yerdos Lohman, Timothy M. Cox, Michael M.
spellingShingle	Petrova, Vessela Chen, Stefanie H. Molzberger, Eileen T. Tomko, Eric Chitteni-Pattu, Sindhu Jia, Haifeng Ordabayev, Yerdos Lohman, Timothy M. Cox, Michael M. Active displacement of RecA filaments by UvrD translocase activity
author_facet	Petrova, Vessela Chen, Stefanie H. Molzberger, Eileen T. Tomko, Eric Chitteni-Pattu, Sindhu Jia, Haifeng Ordabayev, Yerdos Lohman, Timothy M. Cox, Michael M.
author_sort	Petrova, Vessela
title	Active displacement of RecA filaments by UvrD translocase activity
title_short	Active displacement of RecA filaments by UvrD translocase activity
title_full	Active displacement of RecA filaments by UvrD translocase activity
title_fullStr	Active displacement of RecA filaments by UvrD translocase activity
title_full_unstemmed	Active displacement of RecA filaments by UvrD translocase activity
title_sort	active displacement of reca filaments by uvrd translocase activity
description	The UvrD helicase has been implicated in the disassembly of RecA nucleoprotein filaments in vivo and in vitro. We demonstrate that UvrD utilizes an active mechanism to remove RecA from the DNA. Efficient RecA removal depends on the availability of DNA binding sites for UvrD and/or the accessibility of the RecA filament ends. The removal of RecA from DNA also requires ATP hydrolysis by the UvrD helicase but not by RecA protein. The RecA-removal activity of UvrD is slowed by RecA variants with enhanced DNA-binding properties. The ATPase rate of UvrD during RecA removal is much slower than the ATPase activity of UvrD when it is functioning either as a translocase or a helicase on DNA in the absence of RecA. Thus, in this context UvrD may operate in a specialized disassembly mode.
publisher	Oxford University Press
publishDate	2015
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4417151/
_version_	1613218380022546432

Active displacement of RecA filaments by UvrD translocase activity

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