Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
1995-4-5
pubmed:databankReference
pubmed:abstractText
Two rpoN-linked delta Tn10-kan insertions suppress the conditionally lethal erats allele. One truncates rpoN while the second disrupts another gene (ptsN) in the rpoN operon and does not affect classical nitrogen regulation. Neither alter expression of era indicating that suppression is post-translational. Plasmid clones of ptsN prevent suppression by either disruption mutation indicating that this gene is important for lethality caused by erats. rpoN and six neighboring genes were sequenced and compared with sequences in the database. Two of these genes encode proteins homologous to Enzyme IIAFru and HPr of the phosphoenolpyruvate:sugar phosphotransferase system. We designate these proteins IIANtr (ptsN) and NPr (npr). Purified IIANtr and NPr exchange phosphate appropriately with Enzyme I, HPr, and Enzyme IIA proteins of the phosphoenolpyruvate: sugar phosphotransferase system. Several sugars and tricarboxylic acid cycle intermediates inhibited growth of the ptsN disruption mutant on medium containing an amino acid or nucleoside base as a combined source of nitrogen, carbon, and energy. This growth inhibition was relieved by supplying the ptsN gene or ammonium salts but was not aleviated by altering levels of exogenously supplied cAMP. These results support our previous proposal of a novel mechanism linking carbon and nitrogen assimilation and relates IIANtr to the unknown process regulated by the essential GTPase Era.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
3
pubmed:volume
270
pubmed:geneSymbol
npr, ptsN, rpoN
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4822-39
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:7876255-Amino Acid Sequence, pubmed-meshheading:7876255-Base Sequence, pubmed-meshheading:7876255-Cloning, Molecular, pubmed-meshheading:7876255-DNA-Binding Proteins, pubmed-meshheading:7876255-DNA-Directed RNA Polymerases, pubmed-meshheading:7876255-Escherichia coli, pubmed-meshheading:7876255-Escherichia coli Proteins, pubmed-meshheading:7876255-Genes, Lethal, pubmed-meshheading:7876255-Genes, Suppressor, pubmed-meshheading:7876255-Genetic Complementation Test, pubmed-meshheading:7876255-Molecular Sequence Data, pubmed-meshheading:7876255-Mutation, pubmed-meshheading:7876255-Nitrogen, pubmed-meshheading:7876255-Open Reading Frames, pubmed-meshheading:7876255-Operon, pubmed-meshheading:7876255-Phosphoenolpyruvate Sugar Phosphotransferase System, pubmed-meshheading:7876255-Phylogeny, pubmed-meshheading:7876255-RNA Polymerase Sigma 54, pubmed-meshheading:7876255-Sigma Factor, pubmed-meshheading:7876255-Transcription, Genetic
pubmed:year
1995
pubmed:articleTitle
Novel proteins of the phosphotransferase system encoded within the rpoN operon of Escherichia coli. Enzyme IIANtr affects growth on organic nitrogen and the conditional lethality of an erats mutant.
pubmed:affiliation
Laboratory of Chromosome Biology, NCI-Frederick Cancer Research and Development Center, Maryland 21702-1201.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't