Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1995-10-23
pubmed:databankReference
pubmed:abstractText
In Bacillus subtilis, the AhrC protein represses genes encoding enzymes of arginine biosynthesis and activates those mediating its catabolism. To determine how this repressor also functions as an activator, we attempted to clone catabolic genes by searching for insertions of the Tn917-lacZ transposon that express AhrC-dependent, arginine-inducible beta-galactosidase activity. One such isolate was obtained. The region upstream of lacZ was subcloned in Escherichia coli in such a way that it could be replaced in the B. subtilis chromosome after appropriate manipulation. Analysis of exonuclease III-derived deletions located an AhrC-dependent, arginine-inducible promoter to within a ca. 1.9 kb fragment. The sequence revealed: the 3' end of an ORF homologous to gdh genes encoding glutamate dehydrogenase, with highest homology to the homologue from Clostridium difficile; the 5' end of an ORF homologous to a Saccharomyces cerevisiae gene encoding delta 1-pyrroline 5-carboxylate dehydrogenase (P5CDH), an enzyme of arginine catabolism; and just upstream of the latter, a sequence with homology to known AhrC binding sites in the upstream part of the biosynthetic argCJBD-cpa-F cluster. The same region has also been sequenced by others as part of the B. subtilis genome sequencing project, revealing that the P5CDH gene is the first in a cluster termed rocABC. Restriction fragments containing the putative AhrC-binding sequence, but not those lacking it, showed retarded electrophoretic mobility in the presence of purified AhrC. A 277 bp AhrC-binding fragment also showed anomalous mobility in the absence of AhrC, consistent with its being intrinsically bent. DNAse I footprinting localized AhrC binding to bp -16/-22 to +1 (the transcription startpoint). Such a location for an activator binding site, i.e. overlapping the transcription start, is unusual.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0026-8925
pubmed:author
pubmed:issnType
Print
pubmed:day
21
pubmed:volume
248
pubmed:geneSymbol
argR, ghh, lacZ
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
329-40
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:7565595-Amino Acid Sequence, pubmed-meshheading:7565595-Arginine, pubmed-meshheading:7565595-Bacillus subtilis, pubmed-meshheading:7565595-Bacterial Proteins, pubmed-meshheading:7565595-Base Sequence, pubmed-meshheading:7565595-Binding Sites, pubmed-meshheading:7565595-DNA, Bacterial, pubmed-meshheading:7565595-DNA Transposable Elements, pubmed-meshheading:7565595-Deoxyribonuclease I, pubmed-meshheading:7565595-Gene Expression Regulation, Bacterial, pubmed-meshheading:7565595-Genetic Markers, pubmed-meshheading:7565595-Molecular Sequence Data, pubmed-meshheading:7565595-Operon, pubmed-meshheading:7565595-Plasmids, pubmed-meshheading:7565595-Repressor Proteins, pubmed-meshheading:7565595-Sequence Analysis, DNA, pubmed-meshheading:7565595-Sequence Deletion, pubmed-meshheading:7565595-Sequence Homology, Nucleic Acid, pubmed-meshheading:7565595-Transformation, Genetic, pubmed-meshheading:7565595-beta-Galactosidase
pubmed:year
1995
pubmed:articleTitle
A binding site for activation by the Bacillus subtilis AhrC protein, a repressor/activator of arginine metabolism.
pubmed:affiliation
Department of Genetics, University of Leeds, UK.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't