Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
1991-1-24
pubmed:abstractText
A positive, genetic selection against the activity of the nitrogen regulatory (NTR) system was used to isolate insertion mutations affecting nitrogen regulation in Klebsiella aerogenes. Two classes of mutation were obtained: those affecting the NTR system itself and leading to the loss of almost all nitrogen regulation, and those affecting the nac locus and leading to a loss of nitrogen regulation of a family of nitrogen-regulated enzymes. The set of these nac-dependent enzymes included histidase, glutamate dehydrogenase, glutamate synthase, proline oxidase, and urease. The enzymes shown to be nac independent included glutamine synthetase, asparaginase, tryptophan permease, nitrate reductase, the product of the nifLA operon, and perhaps nitrite reductase. The expression of the nac gene was itself highly nitrogen regulated, and this regulation was mediated by the NTR system. The loss of nitrogen regulation was found in each of the four insertion mutants studied, showing that loss of nitrogen regulation resulted from the absence of nac function rather than from an altered form of the nac gene product. Thus we propose two classes of nitrogen-regulated operons: in class I, the NTR system directly activates expression of the operon; in class II, the NTR system activates nac expression and the product(s) of the nac locus activates expression of the operon.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/1979323-14104, http://linkedlifedata.com/resource/pubmed/commentcorrection/1979323-14907713, http://linkedlifedata.com/resource/pubmed/commentcorrection/1979323-18438, http://linkedlifedata.com/resource/pubmed/commentcorrection/1979323-25264, http://linkedlifedata.com/resource/pubmed/commentcorrection/1979323-2563595, http://linkedlifedata.com/resource/pubmed/commentcorrection/1979323-2834335, http://linkedlifedata.com/resource/pubmed/commentcorrection/1979323-2867543, http://linkedlifedata.com/resource/pubmed/commentcorrection/1979323-2874557, http://linkedlifedata.com/resource/pubmed/commentcorrection/1979323-2987183, http://linkedlifedata.com/resource/pubmed/commentcorrection/1979323-2999766, http://linkedlifedata.com/resource/pubmed/commentcorrection/1979323-3142852, http://linkedlifedata.com/resource/pubmed/commentcorrection/1979323-3304660, http://linkedlifedata.com/resource/pubmed/commentcorrection/1979323-3330758, http://linkedlifedata.com/resource/pubmed/commentcorrection/1979323-4145798, http://linkedlifedata.com/resource/pubmed/commentcorrection/1979323-4146916, http://linkedlifedata.com/resource/pubmed/commentcorrection/1979323-4153589, http://linkedlifedata.com/resource/pubmed/commentcorrection/1979323-4331387, http://linkedlifedata.com/resource/pubmed/commentcorrection/1979323-4459, http://linkedlifedata.com/resource/pubmed/commentcorrection/1979323-4598005, http://linkedlifedata.com/resource/pubmed/commentcorrection/1979323-4926673, http://linkedlifedata.com/resource/pubmed/commentcorrection/1979323-6091132, http://linkedlifedata.com/resource/pubmed/commentcorrection/1979323-6109705, http://linkedlifedata.com/resource/pubmed/commentcorrection/1979323-6120932, http://linkedlifedata.com/resource/pubmed/commentcorrection/1979323-6129565, http://linkedlifedata.com/resource/pubmed/commentcorrection/1979323-6130743, http://linkedlifedata.com/resource/pubmed/commentcorrection/1979323-6226649, http://linkedlifedata.com/resource/pubmed/commentcorrection/1979323-6264444, http://linkedlifedata.com/resource/pubmed/commentcorrection/1979323-6324677, http://linkedlifedata.com/resource/pubmed/commentcorrection/1979323-6330041, http://linkedlifedata.com/resource/pubmed/commentcorrection/1979323-6337346, http://linkedlifedata.com/resource/pubmed/commentcorrection/1979323-6352688
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Amino Acid Transport Systems, http://linkedlifedata.com/resource/pubmed/chemical/Asparaginase, http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Glutamate Dehydrogenase, http://linkedlifedata.com/resource/pubmed/chemical/Glutamate-Ammonia Ligase, http://linkedlifedata.com/resource/pubmed/chemical/Histidine Ammonia-Lyase, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Transport Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Nitrate Reductase, http://linkedlifedata.com/resource/pubmed/chemical/Nitrate Reductases, http://linkedlifedata.com/resource/pubmed/chemical/Nitrogen, http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Sigma Factor, http://linkedlifedata.com/resource/pubmed/chemical/TAT2 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/TnaB protein, E coli, http://linkedlifedata.com/resource/pubmed/chemical/Urease, http://linkedlifedata.com/resource/pubmed/chemical/beta-Galactosidase
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-9193
pubmed:author
pubmed:issnType
Print
pubmed:volume
172
pubmed:geneSymbol
nac, ntrB, ntrC, rpoN
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7249-55
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed-meshheading:1979323-Amino Acid Transport Systems, pubmed-meshheading:1979323-Asparaginase, pubmed-meshheading:1979323-Escherichia coli Proteins, pubmed-meshheading:1979323-Gene Expression Regulation, Bacterial, pubmed-meshheading:1979323-Glutamate Dehydrogenase, pubmed-meshheading:1979323-Glutamate-Ammonia Ligase, pubmed-meshheading:1979323-Histidine Ammonia-Lyase, pubmed-meshheading:1979323-Klebsiella pneumoniae, pubmed-meshheading:1979323-Membrane Transport Proteins, pubmed-meshheading:1979323-Mutation, pubmed-meshheading:1979323-Nitrate Reductase, pubmed-meshheading:1979323-Nitrate Reductases, pubmed-meshheading:1979323-Nitrogen, pubmed-meshheading:1979323-Operon, pubmed-meshheading:1979323-Saccharomyces cerevisiae Proteins, pubmed-meshheading:1979323-Sigma Factor, pubmed-meshheading:1979323-Urease, pubmed-meshheading:1979323-beta-Galactosidase
pubmed:year
1990
pubmed:articleTitle
Role of the nac gene product in the nitrogen regulation of some NTR-regulated operons of Klebsiella aerogenes.
pubmed:affiliation
Department of Biology, University of Michigan, Ann Arbor 48109.
pubmed:publicationType
Journal Article
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