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dc.contributor.authorLobner-Olesen, Anders
dc.contributor.authorMarinus, Martin G.
dc.date2022-08-11T08:08:00.000
dc.date.accessioned2022-08-23T15:39:09Z
dc.date.available2022-08-23T15:39:09Z
dc.date.issued1992-01-01
dc.date.submitted2009-01-12
dc.identifier.citation<p>J Bacteriol. 1992 Jan;174(2):525-9.</p>
dc.identifier.issn0021-9193 (Print)
dc.identifier.doi10.1128/jb.174.2.525-529.1992
dc.identifier.pmid1309529
dc.identifier.urihttp://hdl.handle.net/20.500.14038/26098
dc.description.abstractDNA sequence analysis has revealed that an unidentified open reading frame (ufr1) is present immediately preceding the aroB gene of Escherichia coli. The predicted protein product of urf1 contains a consensus ATP-binding-site sequence and shows 34% amino acid homology to shikimate kinase II in a 97-amino-acid region. Inactivation of urf1 by insertion of an antibiotic resistance gene had a polar effect on aroB, indicating that these two genes constitute a transcriptional unit. The auxotrophic requirements of a strain mutant for both urf1 and aroL (encoding shikimate kinase II) are consistent with shikimate kinase deficiency. We propose that urf1 encodes shikimate kinase I and that it be designated aroK.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=1309529&dopt=Abstract">Link to Article in PubMed</a></p>
dc.relation.urlhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC205746/?tool=pubmed
dc.subjectAmino Acid Sequence
dc.subjectBase Sequence
dc.subjectChromosomes, Bacterial
dc.subjectCloning, Molecular
dc.subjectDNA Transposable Elements
dc.subjectEscherichia coli
dc.subject*Genes, Bacterial
dc.subjectLac Operon
dc.subjectMolecular Sequence Data
dc.subjectMutation
dc.subjectOpen Reading Frames
dc.subjectPhosphotransferases
dc.subject*Phosphotransferases (Alcohol Group Acceptor)
dc.subjectTranscription, Genetic
dc.subjectBacteria
dc.subjectBiochemistry, Biophysics, and Structural Biology
dc.subjectEnzymes and Coenzymes
dc.subjectGenetic Phenomena
dc.subjectPharmacology, Toxicology and Environmental Health
dc.titleIdentification of the gene (aroK) encoding shikimic acid kinase I of Escherichia coli
dc.typeJournal Article
dc.source.journaltitleJournal of bacteriology
dc.source.volume174
dc.source.issue2
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/bmp_pp/38
dc.identifier.contextkey692454
html.description.abstract<p>DNA sequence analysis has revealed that an unidentified open reading frame (ufr1) is present immediately preceding the aroB gene of Escherichia coli. The predicted protein product of urf1 contains a consensus ATP-binding-site sequence and shows 34% amino acid homology to shikimate kinase II in a 97-amino-acid region. Inactivation of urf1 by insertion of an antibiotic resistance gene had a polar effect on aroB, indicating that these two genes constitute a transcriptional unit. The auxotrophic requirements of a strain mutant for both urf1 and aroL (encoding shikimate kinase II) are consistent with shikimate kinase deficiency. We propose that urf1 encodes shikimate kinase I and that it be designated aroK.</p>
dc.identifier.submissionpathbmp_pp/38
dc.contributor.departmentDepartment of Biochemistry and Molecular Pharmacology
dc.source.pages525-9


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