Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2002-6-19
pubmed:abstractText
The heterotrimeric RecBCD enzyme of Escherichia coli is required for the major pathway of double-strand DNA break repair and genetic exchange. Assembled as a heterotrimer, the enzyme has potent nuclease and helicase activity. Analysis of recC nonsense and deletion mutations revealed that the C terminus of RecC is required for assembly of the RecD subunit into RecBCD holoenzyme but not for recombination proficiency; the phenotype of these mutations mimics that of recD deletion mutations. Partial proteolysis of purified RecC polypeptide yielded a C-terminal fragment that corresponds to the RecD-interaction domain. RecD is essential for nuclease activity, regulation by the recombination hotspot Chi, and high affinity for DNA ends. The RecC-RecD interface thus appears critical for the regulation of RecBCD enzyme via the assembly and, we propose, disassembly or conformational change of the RecD subunit.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/12072448-10197988, http://linkedlifedata.com/resource/pubmed/commentcorrection/12072448-10197989, http://linkedlifedata.com/resource/pubmed/commentcorrection/12072448-10480929, http://linkedlifedata.com/resource/pubmed/commentcorrection/12072448-10766864, http://linkedlifedata.com/resource/pubmed/commentcorrection/12072448-10840065, http://linkedlifedata.com/resource/pubmed/commentcorrection/12072448-10884344, http://linkedlifedata.com/resource/pubmed/commentcorrection/12072448-11700284, http://linkedlifedata.com/resource/pubmed/commentcorrection/12072448-1310498, http://linkedlifedata.com/resource/pubmed/commentcorrection/12072448-1311326, http://linkedlifedata.com/resource/pubmed/commentcorrection/12072448-1535156, http://linkedlifedata.com/resource/pubmed/commentcorrection/12072448-1737764, http://linkedlifedata.com/resource/pubmed/commentcorrection/12072448-1855256, http://linkedlifedata.com/resource/pubmed/commentcorrection/12072448-2172076, http://linkedlifedata.com/resource/pubmed/commentcorrection/12072448-2249753, http://linkedlifedata.com/resource/pubmed/commentcorrection/12072448-3155726, http://linkedlifedata.com/resource/pubmed/commentcorrection/12072448-319095, http://linkedlifedata.com/resource/pubmed/commentcorrection/12072448-3298248, http://linkedlifedata.com/resource/pubmed/commentcorrection/12072448-3520484, http://linkedlifedata.com/resource/pubmed/commentcorrection/12072448-3526335, http://linkedlifedata.com/resource/pubmed/commentcorrection/12072448-3537961, http://linkedlifedata.com/resource/pubmed/commentcorrection/12072448-3611052, http://linkedlifedata.com/resource/pubmed/commentcorrection/12072448-3888404, http://linkedlifedata.com/resource/pubmed/commentcorrection/12072448-3888405, http://linkedlifedata.com/resource/pubmed/commentcorrection/12072448-4562227, http://linkedlifedata.com/resource/pubmed/commentcorrection/12072448-4884815, http://linkedlifedata.com/resource/pubmed/commentcorrection/12072448-5335129, http://linkedlifedata.com/resource/pubmed/commentcorrection/12072448-592405, http://linkedlifedata.com/resource/pubmed/commentcorrection/12072448-6348024, http://linkedlifedata.com/resource/pubmed/commentcorrection/12072448-6393130, http://linkedlifedata.com/resource/pubmed/commentcorrection/12072448-7592660, http://linkedlifedata.com/resource/pubmed/commentcorrection/12072448-7968921, http://linkedlifedata.com/resource/pubmed/commentcorrection/12072448-8384931, http://linkedlifedata.com/resource/pubmed/commentcorrection/12072448-8387820, http://linkedlifedata.com/resource/pubmed/commentcorrection/12072448-9230304, http://linkedlifedata.com/resource/pubmed/commentcorrection/12072448-9348042, http://linkedlifedata.com/resource/pubmed/commentcorrection/12072448-9448271, http://linkedlifedata.com/resource/pubmed/commentcorrection/12072448-9790841
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0016-6731
pubmed:author
pubmed:issnType
Print
pubmed:volume
161
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
483-92
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
A domain of RecC required for assembly of the regulatory RecD subunit into the Escherichia coli RecBCD holoenzyme.
pubmed:affiliation
Fred Hutchinson Cancer Research Center, Seattle, Washington 98109, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.