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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
23
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pubmed:dateCreated |
1994-12-27
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pubmed:databankReference |
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pubmed:abstractText |
An Escherichia coli strain with thermosensitive expression of the gene encoding peptide deformylase (fms) has been constructed. At nonpermissive temperatures, this strain fails to grow. The essential character of the fms gene was further used to clone by heterologous complementation the locus corresponding to Thermus thermophilus peptide deformylase. The cloned fragment also carries the methionyl-tRNA(fMet) formyltransferase gene (fmt). It is located immediately downstream from the fms gene, as in E. coli. Further sequence analysis of the region surrounding the E. coli fms-fmt locus indicates that the genes bordering the fms-fmt region are not conserved in T. thermophilus.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/7961514-1624424,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7961514-2200508,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7961514-2257496,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7961514-2544569,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7961514-2548993,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7961514-2670909,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7961514-2695747,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7961514-2914602,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7961514-2989779,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7961514-3038334,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7961514-3139093,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7961514-3162770,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7961514-4887858,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7961514-4970729,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7961514-4973445,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7961514-6249792,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7961514-6251971,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7961514-8112305,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7961514-8199241,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7961514-8226647,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7961514-8244948,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7961514-8432722,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7961514-8501063
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0021-9193
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
176
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pubmed:geneSymbol |
fms,
fmt,
trkA
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
7387-90
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:7961514-Acyltransferases,
pubmed-meshheading:7961514-Amidohydrolases,
pubmed-meshheading:7961514-Amino Acid Sequence,
pubmed-meshheading:7961514-Aminopeptidases,
pubmed-meshheading:7961514-Carrier Proteins,
pubmed-meshheading:7961514-Cloning, Molecular,
pubmed-meshheading:7961514-Escherichia coli,
pubmed-meshheading:7961514-Genes, Bacterial,
pubmed-meshheading:7961514-Genes, Lethal,
pubmed-meshheading:7961514-Hydroxymethyl and Formyl Transferases,
pubmed-meshheading:7961514-Membrane Proteins,
pubmed-meshheading:7961514-Molecular Sequence Data,
pubmed-meshheading:7961514-Mutation,
pubmed-meshheading:7961514-Receptor, trkA,
pubmed-meshheading:7961514-Restriction Mapping,
pubmed-meshheading:7961514-Sequence Analysis, DNA,
pubmed-meshheading:7961514-Sequence Homology, Amino Acid,
pubmed-meshheading:7961514-Thermus thermophilus
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pubmed:year |
1994
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pubmed:articleTitle |
Characterization of the Thermus thermophilus locus encoding peptide deformylase and methionyl-tRNA(fMet) formyltransferase.
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pubmed:affiliation |
Laboratoire de Biochimie, Unité de Recherche Associée no. 240 du Centre National de la Recherche Scientifique, Ecole Polytechnique, Palaiseau, France.
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pubmed:publicationType |
Journal Article,
Comparative Study
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