Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
13
pubmed:dateCreated
2001-6-7
pubmed:abstractText
Lrp (leucine-responsive regulatory protein) plays a global regulatory role in Escherichia coli, affecting expression of dozens of operons. Numerous lrp-related genes have been identified in different bacteria and archaea, including asnC, an E. coli gene that was the first reported member of this family. Pairwise comparisons of amino acid sequences of the corresponding proteins shows an average sequence identity of only 29% for the vast majority of comparisons. By contrast, Lrp-related proteins from enteric bacteria show more than 97% amino acid identity. Is the global regulatory role associated with E. coli Lrp limited to enteric bacteria? To probe this question we investigated LrfB, an Lrp-related protein from Haemophilus influenzae that shares 75% sequence identity with E. coli Lrp (highest sequence identity among 42 sequences compared). A strain of H. influenzae having an lrfB null allele grew at the wild-type growth rate but with a filamentous morphology. A comparison of two-dimensional (2D) electrophoretic patterns of proteins from parent and mutant strains showed only two differences (comparable studies with lrp(+) and lrp E. coli strains by others showed 20 differences). The abundance of LrfB in H. influenzae, estimated by Western blotting experiments, was about 130 dimers per cell (compared to 3,000 dimers per E. coli cell). LrfB expressed in E. coli replaced Lrp as a repressor of the lrp gene but acted only to a limited extent as an activator of the ilvIH operon. Thus, although LrfB resembles Lrp sufficiently to perform some of its functions, its low abundance is consonant with a more local role in regulating but a few genes, a view consistent with the results of the 2D electrophoretic analysis. We speculate that an Lrp having a global regulatory role evolved to help enteric bacteria adapt to their ecological niches and that it is unlikely that Lrp-related proteins in other organisms have a broad regulatory function.
pubmed:grant
pubmed:commentsCorrections
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pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0021-9193
pubmed:author
pubmed:issnType
Print
pubmed:volume
183
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4004-11
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed-meshheading:11395465-Acetolactate Synthase, pubmed-meshheading:11395465-Amino Acid Sequence, pubmed-meshheading:11395465-Bacterial Proteins, pubmed-meshheading:11395465-DNA-Binding Proteins, pubmed-meshheading:11395465-Escherichia coli Proteins, pubmed-meshheading:11395465-Gene Expression Profiling, pubmed-meshheading:11395465-Gene Expression Regulation, Bacterial, pubmed-meshheading:11395465-Genes, Bacterial, pubmed-meshheading:11395465-Haemophilus influenzae, pubmed-meshheading:11395465-Leucine-Responsive Regulatory Protein, pubmed-meshheading:11395465-Molecular Sequence Data, pubmed-meshheading:11395465-Mutation, pubmed-meshheading:11395465-Phenotype, pubmed-meshheading:11395465-Protein Binding, pubmed-meshheading:11395465-Sequence Homology, Amino Acid, pubmed-meshheading:11395465-Transcription Factors
pubmed:year
2001
pubmed:articleTitle
Global versus local regulatory roles for Lrp-related proteins: Haemophilus influenzae as a case study.
pubmed:affiliation
Section of Biochemistry, Molecular and Cell Biology, Cornell University, Ithaca, New York 14853, USA.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S.