Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
18
pubmed:dateCreated
1994-10-12
pubmed:abstractText
Phase variation of type 1 fimbriation in Escherichia coli is associated with the site-specific recombination of a 314-bp DNA invertible element. The fim switch directs transcription of fimA, the major fimbrial subunit gene, in one orientation (on) but not the other (off). Switching requires either fimB (on-to-off or off-to-on inversion) or fimE (on-to-off inversion only) and is reduced sharply in strains containing lrp::Tn10 mutations. Both fimE-promoted switching and fimB-promoted switching are stimulated by the amino acids alanine, isoleucine, leucine, and valine, and this regulation requires lrp. Here it is shown that the leucine-responsive regulatory protein (Lrp) binds in and adjacent to the fim switch. Mutations in fim that lower Lrp binding in vitro have corresponding effects on both fimB-promoted switching and fimE-promoted switching in vivo. Lrp initiates binding at one of two sites within the fim switch. Additional cooperative binding results in an extensive region of protection from both DNase I and 1,10-phenanthroline-copper complex-activated DNA cleavage. The region of protection can extend to within 12 bp of the right inverted repeat (switch off) and occupies over one-third of the switch. It is proposed that wrapping of fim DNA around an Lrp complex is required to form a recombination-proficient structure.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/7916011-1346534, http://linkedlifedata.com/resource/pubmed/commentcorrection/7916011-1350087, http://linkedlifedata.com/resource/pubmed/commentcorrection/7916011-1648076, http://linkedlifedata.com/resource/pubmed/commentcorrection/7916011-1679429, http://linkedlifedata.com/resource/pubmed/commentcorrection/7916011-1679430, http://linkedlifedata.com/resource/pubmed/commentcorrection/7916011-1686293, http://linkedlifedata.com/resource/pubmed/commentcorrection/7916011-1779842, http://linkedlifedata.com/resource/pubmed/commentcorrection/7916011-2040596, http://linkedlifedata.com/resource/pubmed/commentcorrection/7916011-2115869, http://linkedlifedata.com/resource/pubmed/commentcorrection/7916011-2863818, http://linkedlifedata.com/resource/pubmed/commentcorrection/7916011-2874022, http://linkedlifedata.com/resource/pubmed/commentcorrection/7916011-2886490, http://linkedlifedata.com/resource/pubmed/commentcorrection/7916011-2888114, http://linkedlifedata.com/resource/pubmed/commentcorrection/7916011-4604283, http://linkedlifedata.com/resource/pubmed/commentcorrection/7916011-6271456, http://linkedlifedata.com/resource/pubmed/commentcorrection/7916011-7901196, http://linkedlifedata.com/resource/pubmed/commentcorrection/7916011-8093239, http://linkedlifedata.com/resource/pubmed/commentcorrection/7916011-8096319, http://linkedlifedata.com/resource/pubmed/commentcorrection/7916011-8101185, http://linkedlifedata.com/resource/pubmed/commentcorrection/7916011-8104927, http://linkedlifedata.com/resource/pubmed/commentcorrection/7916011-8429549, http://linkedlifedata.com/resource/pubmed/commentcorrection/7916011-8508774
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins, http://linkedlifedata.com/resource/pubmed/chemical/DNA, Bacterial, http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Fimbriae Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Integrases, http://linkedlifedata.com/resource/pubmed/chemical/Leucine-Responsive Regulatory..., http://linkedlifedata.com/resource/pubmed/chemical/Lrp protein, E coli, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors, http://linkedlifedata.com/resource/pubmed/chemical/fimB protein, E coli, http://linkedlifedata.com/resource/pubmed/chemical/fimE protein, E coli, http://linkedlifedata.com/resource/pubmed/chemical/fimbrillin
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0021-9193
pubmed:author
pubmed:issnType
Print
pubmed:volume
176
pubmed:geneSymbol
fimA, fimB, fimE, lrp
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5665-72
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed-meshheading:7916011-Bacterial Proteins, pubmed-meshheading:7916011-Base Sequence, pubmed-meshheading:7916011-Binding Sites, pubmed-meshheading:7916011-DNA, Bacterial, pubmed-meshheading:7916011-DNA-Binding Proteins, pubmed-meshheading:7916011-Escherichia coli, pubmed-meshheading:7916011-Escherichia coli Proteins, pubmed-meshheading:7916011-Fimbriae, Bacterial, pubmed-meshheading:7916011-Fimbriae Proteins, pubmed-meshheading:7916011-Gene Expression Regulation, Bacterial, pubmed-meshheading:7916011-Integrases, pubmed-meshheading:7916011-Leucine-Responsive Regulatory Protein, pubmed-meshheading:7916011-Molecular Sequence Data, pubmed-meshheading:7916011-Mutation, pubmed-meshheading:7916011-Recombination, Genetic, pubmed-meshheading:7916011-Transcription, Genetic, pubmed-meshheading:7916011-Transcription Factors
pubmed:year
1994
pubmed:articleTitle
The leucine-responsive regulatory protein binds to the fim switch to control phase variation of type 1 fimbrial expression in Escherichia coli K-12.
pubmed:affiliation
Department of Microbiology and Immunology, Bowman Gray School of Medicine, Winston-Salem, North Carolina 27157-1064.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't