Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
15
pubmed:dateCreated
1992-6-25
pubmed:databankReference
pubmed:abstractText
The DNA sequence of the sulfate activation locus from Escherichia coli K-12 has been determined. The sequence includes the structural genes encoding the enzymes ATP sulfurylase (cysD and cysN) and APS kinase (cysC) which catalyze the synthesis of activated sulfate. These are the only genes known to reside in the sulfate activation operon. Consensus elements of the operon promoter were identified, and the start codons and open reading frames of the Cys polypeptides were determined. During this work, another gene, iap, was partially sequenced and mapped. The activity of ATP sulfurylase is stimulated by an intrinsic GTPase. Comparison of the primary sequences of CysN and Ef-Tu revealed that CysN has conserved many of the residues integral to the three-dimensional structure important for guanine nucleotide binding in Ef-Tu and RAS. nodP and nodQ, from Rhizobium meliloti, are essential for nodulation in leguminous plants. The Cys and Nod proteins are remarkably similar. NodP appears to be the smaller subunit of ATP sulfurylase. NodQ encodes homologues of both CysN and CysC; thus, these enzymes may be covalently associated in R. meliloti. The consensus GTP-binding sequences of NodQ and CysN are identical suggesting that NodQ encodes a regulatory GTPase.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
267
pubmed:geneSymbol
cysC, cysD, cysN, iap, nodP, nodQ
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
10405-10
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:1316900-Amino Acid Sequence, pubmed-meshheading:1316900-Base Sequence, pubmed-meshheading:1316900-Chromosome Mapping, pubmed-meshheading:1316900-Codon, pubmed-meshheading:1316900-DNA, Bacterial, pubmed-meshheading:1316900-Escherichia coli, pubmed-meshheading:1316900-Genes, Bacterial, pubmed-meshheading:1316900-Molecular Sequence Data, pubmed-meshheading:1316900-Open Reading Frames, pubmed-meshheading:1316900-Operon, pubmed-meshheading:1316900-Peptide Elongation Factor Tu, pubmed-meshheading:1316900-Phosphotransferases, pubmed-meshheading:1316900-Phosphotransferases (Alcohol Group Acceptor), pubmed-meshheading:1316900-Promoter Regions, Genetic, pubmed-meshheading:1316900-Protein Biosynthesis, pubmed-meshheading:1316900-Restriction Mapping, pubmed-meshheading:1316900-Sequence Alignment, pubmed-meshheading:1316900-Sulfate Adenylyltransferase, pubmed-meshheading:1316900-Sulfates, pubmed-meshheading:1316900-Terminator Regions, Genetic
pubmed:year
1992
pubmed:articleTitle
The DNA sequence of the sulfate activation locus from Escherichia coli K-12.
pubmed:affiliation
Department of Biochemistry, Albert Einstein College of Medicine, Bronx, New York 10461.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.