rdf:type |
|
lifeskim:mentions |
umls-concept:C0014834,
umls-concept:C0017262,
umls-concept:C0125575,
umls-concept:C0185117,
umls-concept:C0205390,
umls-concept:C0205419,
umls-concept:C0332307,
umls-concept:C0814810,
umls-concept:C1145667,
umls-concept:C1707719,
umls-concept:C2587213,
umls-concept:C2911684
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pubmed:issue |
18
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pubmed:dateCreated |
1994-10-12
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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.
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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
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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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
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0021-9193
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:volume |
176
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pubmed:geneSymbol |
fimA,
fimB,
fimE,
lrp
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
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pubmed:pagination |
5665-72
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pubmed:dateRevised |
2009-11-18
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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
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pubmed:year |
1994
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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.
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pubmed:affiliation |
Department of Microbiology and Immunology, Bowman Gray School of Medicine, Winston-Salem, North Carolina 27157-1064.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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