12730132

Source:http://linkedlifedata.com/resource/pubmed/id/12730132

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0012860, umls-concept:C0205275, umls-concept:C0218063, umls-concept:C1261381, umls-concept:C1710082
pubmed:issue	9
pubmed:dateCreated	2003-5-5
pubmed:abstractText	The DNA-damage response genes in bacteria are up-regulated when LexA repressor undergoes autocatalytic cleavage stimulated by activated RecA protein. Intact LexA is stable to intracellular degradation but its auto-cleavage fragments are degraded rapidly. Here, both fragments of LexA are shown to be substrates for the ClpXP protease. ClpXP recognizes these fragments using sequence motifs that flank the auto-cleavage site but are dormant in intact LexA. Furthermore, ClpXP degradation of the LexA-DNA-binding fragment is important to cell survival after DNA damage. These results demonstrate how one protein-processing event can activate latent protease recognition signals, triggering a cascade of protein turnover in response to environmental stress.
pubmed:grant	http://linkedlifedata.com/resource/pubmed/grant/AI-16892, http://linkedlifedata.com/resource/pubmed/grant/R01 GM049224-11
pubmed:commentsCorrections	http://linkedlifedata.com/resource/pubmed/commentcorrection/12730132-10318812, http://linkedlifedata.com/resource/pubmed/commentcorrection/12730132-10882100, http://linkedlifedata.com/resource/pubmed/commentcorrection/12730132-11238382, http://linkedlifedata.com/resource/pubmed/commentcorrection/12730132-11535833, http://linkedlifedata.com/resource/pubmed/commentcorrection/12730132-11551506, http://linkedlifedata.com/resource/pubmed/commentcorrection/12730132-12057945, http://linkedlifedata.com/resource/pubmed/commentcorrection/12730132-12183369, http://linkedlifedata.com/resource/pubmed/commentcorrection/12730132-1911752, http://linkedlifedata.com/resource/pubmed/commentcorrection/12730132-3063828, http://linkedlifedata.com/resource/pubmed/commentcorrection/12730132-6231641, http://linkedlifedata.com/resource/pubmed/commentcorrection/12730132-6272195, http://linkedlifedata.com/resource/pubmed/commentcorrection/12730132-6300834, http://linkedlifedata.com/resource/pubmed/commentcorrection/12730132-6410076, http://linkedlifedata.com/resource/pubmed/commentcorrection/12730132-6461657, http://linkedlifedata.com/resource/pubmed/commentcorrection/12730132-7023697, http://linkedlifedata.com/resource/pubmed/commentcorrection/12730132-7536743, http://linkedlifedata.com/resource/pubmed/commentcorrection/12730132-7557391, http://linkedlifedata.com/resource/pubmed/commentcorrection/12730132-7845214, http://linkedlifedata.com/resource/pubmed/commentcorrection/12730132-8298465, http://linkedlifedata.com/resource/pubmed/commentcorrection/12730132-8584937, http://linkedlifedata.com/resource/pubmed/commentcorrection/12730132-8876169, http://linkedlifedata.com/resource/pubmed/commentcorrection/12730132-8982462, http://linkedlifedata.com/resource/pubmed/commentcorrection/12730132-9573050, http://linkedlifedata.com/resource/pubmed/commentcorrection/12730132-9643546
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/8711660
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases, http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins, http://linkedlifedata.com/resource/pubmed/chemical/ClpX protein, E coli, http://linkedlifedata.com/resource/pubmed/chemical/Endopeptidase Clp, http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins, http://linkedlifedata.com/resource/pubmed/chemical/LexA protein, Bacteria, http://linkedlifedata.com/resource/pubmed/chemical/Molecular Chaperones, http://linkedlifedata.com/resource/pubmed/chemical/Peptides, http://linkedlifedata.com/resource/pubmed/chemical/Serine Endopeptidases
pubmed:status	MEDLINE
pubmed:month	May
pubmed:issn	0890-9369
pubmed:author	pubmed-author:BakerTania ATA, pubmed-author:FlynnJulia MJM, pubmed-author:NeherSaskia BSB, pubmed-author:SauerRobert TRT
pubmed:issnType	Print
pubmed:day	1
pubmed:volume	17
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	1084-9
pubmed:dateRevised	2011-1-25
pubmed:meshHeading	pubmed-meshheading:12730132-Adenosine Triphosphatases, pubmed-meshheading:12730132-Bacterial Proteins, pubmed-meshheading:12730132-Cell Survival, pubmed-meshheading:12730132-DNA Damage, pubmed-meshheading:12730132-Endopeptidase Clp, pubmed-meshheading:12730132-Escherichia coli Proteins, pubmed-meshheading:12730132-Molecular Chaperones, pubmed-meshheading:12730132-Peptides, pubmed-meshheading:12730132-Serine Endopeptidases, pubmed-meshheading:12730132-Ultraviolet Rays
pubmed:year	2003
pubmed:articleTitle	Latent ClpX-recognition signals ensure LexA destruction after DNA damage.
pubmed:affiliation	Department of Biology and Howard Hughes Medical Institute, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.
pubmed:publicationType	Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't