Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
23
pubmed:dateCreated
1985-1-10
pubmed:databankReference
pubmed:abstractText
Regulation of the Escherichia coli dapD gene involved in diaminopimelate and lysine biosynthesis was unknown as no convenient enzymatic assay was available until recently. This gene was cloned into pBR322 from a lambda transducing phage; its complete nucleotide sequence was established. This sequence shows that the dapD gene is composed of a single cistron encoding a 274-amino acid polypeptide, Mr 30,040. Enzymatic activity measurements show that this gene encodes the tetrahydrodipicolinate N-succinyltransferase which catalyzes the third step of the specific lysine-diaminopimelate pathway. The transcriptional start of the dapD gene was localized; the identified promoter signals are weak compared to those from the E. coli promoter consensus sequence. The dapD gene-coding sequence is followed by a typical rho-independent transcriptional termination sequence. A study using an operon fusion constructed in vitro between the dapD promoter and the galK structural gene indicated that dapD gene expression is repressed by lysine; no attenuation-like sequence can be found to account for this regulation. At the present time, out of the 9 genes involved in diaminopimelate and lysine biosynthesis, 6 are known to be lysine regulated.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
259
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
14824-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
Regulation of expression and nucleotide sequence of the Escherichia coli dapD gene.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't