Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1998-3-19
pubmed:abstractText
The activity of a number of proteins is regulated by self-processing reactions. Elegant examples are the cleavage of the prokaryotic LexA and lambdaCI transcriptional repressors and the UmuD-like mutagenesis proteins. Various studies support the hypothesis that LexA and lambdaCI cleavage reactions are predominantly intramolecular in nature. The recently described crystal structure of the Escherichia coli UmuD' protein (the posttranslational cleavage product of the UmuD protein) suggests, however, that the region of the protein corresponding to the cleavage site is at least 50 A away from the catalytic active site. We considered the possibility, therefore, that the UmuD-like proteins might undergo self-processing that, in contrast to LexA and lambdaCI, occurs via an intermolecular rather than intramolecular reaction. To test this hypothesis, we introduced into E. coli compatible plasmids with mutations at either the cleavage or the catalytic site of three UmuD-like proteins. Cleavage of these proteins only occurs in the presence of both plasmids, indicating that the reaction is indeed intermolecular in nature. Furthermore, this intermolecular reaction is completely dependent upon the multifunctional RecA protein and leads to the restoration of cellular mutagenesis in nonmutable E. coli strains. Intermolecular cleavage of a biotinylated UmuD active site mutant was also observed in vitro in the presence of the wild-type UmuD' protein, indicating that in addition to the intact UmuD protein, the normal cleavage product (UmuD') can also act as a classical enzyme.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/9465040-1400235, http://linkedlifedata.com/resource/pubmed/commentcorrection/9465040-1438275, http://linkedlifedata.com/resource/pubmed/commentcorrection/9465040-1654503, http://linkedlifedata.com/resource/pubmed/commentcorrection/9465040-2006191, http://linkedlifedata.com/resource/pubmed/commentcorrection/9465040-2188949, http://linkedlifedata.com/resource/pubmed/commentcorrection/9465040-2277636, http://linkedlifedata.com/resource/pubmed/commentcorrection/9465040-2522996, http://linkedlifedata.com/resource/pubmed/commentcorrection/9465040-2693734, http://linkedlifedata.com/resource/pubmed/commentcorrection/9465040-2948553, http://linkedlifedata.com/resource/pubmed/commentcorrection/9465040-3108885, http://linkedlifedata.com/resource/pubmed/commentcorrection/9465040-3126496, http://linkedlifedata.com/resource/pubmed/commentcorrection/9465040-3279417, http://linkedlifedata.com/resource/pubmed/commentcorrection/9465040-3279418, http://linkedlifedata.com/resource/pubmed/commentcorrection/9465040-3542969, http://linkedlifedata.com/resource/pubmed/commentcorrection/9465040-3889923, http://linkedlifedata.com/resource/pubmed/commentcorrection/9465040-6098521, http://linkedlifedata.com/resource/pubmed/commentcorrection/9465040-6211591, http://linkedlifedata.com/resource/pubmed/commentcorrection/9465040-6231641, http://linkedlifedata.com/resource/pubmed/commentcorrection/9465040-8051014, http://linkedlifedata.com/resource/pubmed/commentcorrection/9465040-8349538, http://linkedlifedata.com/resource/pubmed/commentcorrection/9465040-8366028, http://linkedlifedata.com/resource/pubmed/commentcorrection/9465040-8367479, http://linkedlifedata.com/resource/pubmed/commentcorrection/9465040-8513500, http://linkedlifedata.com/resource/pubmed/commentcorrection/9465040-8614470, http://linkedlifedata.com/resource/pubmed/commentcorrection/9465040-8658137, http://linkedlifedata.com/resource/pubmed/commentcorrection/9465040-8755866, http://linkedlifedata.com/resource/pubmed/commentcorrection/9465040-8816793, http://linkedlifedata.com/resource/pubmed/commentcorrection/9465040-9236122, http://linkedlifedata.com/resource/pubmed/commentcorrection/9465040-9406544
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:day
17
pubmed:volume
95
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1478-83
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Intermolecular cleavage by UmuD-like mutagenesis proteins.
pubmed:affiliation
Section on DNA Replication, Repair, and Mutagenesis, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892-2725, USA.
pubmed:publicationType
Journal Article