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http://purl.uniprot.org/citations/8617268http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8617268http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8617268http://www.w3.org/2000/01/rdf-schema#comment"The gene encoding the elongation factor Ts from Thermus thermophilus was sequenced, cloned and the protein overproduced in Escherichia coli. In comparison to the EF-Ts from E. coli with 282 amino acid residues, EF-Ts from T. thermophilus is considerably shorter, differing by 86 amino acids. EF-Ts from the thermophile is stable at high temperatures, which facilitates its separation from E. coli proteins. Purified T. thermophilus EF-Ts forms a homodimer with a disulfide bridge between the two cysteine residues at position 190. The modification of Cys19O by iodoacetamide affects neither the dimerization nor the ability of EF-Ts to facilitate the nucleotide exchange of elongation factor Tu. The disulfide bridge was detected only in purified EF-TS, but not in protein extracts immediately after cell disruption. The physiological role of this disulfide bridge remains, therefore, unclear. Besides the quaternary (EF-TU . EF-Ts)2 complex, a ternary EF-TU . EF-Ts2 complex was detected by gel permeation chromatography and polyacrylamide gel electrophoresis. Trypsin cleavage after Lys48 or modification of Cys78 yield inactive EF-Ts, that does not bind to EF-Tu but is still capable of forming homodimers."xsd:string
http://purl.uniprot.org/citations/8617268http://purl.org/dc/terms/identifier"doi:10.1111/j.1432-1033.1996.00222.x"xsd:string
http://purl.uniprot.org/citations/8617268http://purl.org/dc/terms/identifier"doi:10.1111/j.1432-1033.1996.00222.x"xsd:string
http://purl.uniprot.org/citations/8617268http://purl.uniprot.org/core/author"Blank J."xsd:string
http://purl.uniprot.org/citations/8617268http://purl.uniprot.org/core/author"Blank J."xsd:string
http://purl.uniprot.org/citations/8617268http://purl.uniprot.org/core/author"Kreutzer R."xsd:string
http://purl.uniprot.org/citations/8617268http://purl.uniprot.org/core/author"Kreutzer R."xsd:string
http://purl.uniprot.org/citations/8617268http://purl.uniprot.org/core/author"Nock S."xsd:string
http://purl.uniprot.org/citations/8617268http://purl.uniprot.org/core/author"Nock S."xsd:string
http://purl.uniprot.org/citations/8617268http://purl.uniprot.org/core/author"Sprinzl M."xsd:string
http://purl.uniprot.org/citations/8617268http://purl.uniprot.org/core/author"Sprinzl M."xsd:string
http://purl.uniprot.org/citations/8617268http://purl.uniprot.org/core/date"1996"xsd:gYear
http://purl.uniprot.org/citations/8617268http://purl.uniprot.org/core/date"1996"xsd:gYear
http://purl.uniprot.org/citations/8617268http://purl.uniprot.org/core/name"Eur. J. Biochem."xsd:string
http://purl.uniprot.org/citations/8617268http://purl.uniprot.org/core/name"Eur. J. Biochem."xsd:string
http://purl.uniprot.org/citations/8617268http://purl.uniprot.org/core/pages"222-227"xsd:string
http://purl.uniprot.org/citations/8617268http://purl.uniprot.org/core/pages"222-227"xsd:string
http://purl.uniprot.org/citations/8617268http://purl.uniprot.org/core/title"Elongation factor Ts from Thermus thermophilus -- overproduction in Escherichia coli, quaternary structure and interaction with elongation factor Tu."xsd:string
http://purl.uniprot.org/citations/8617268http://purl.uniprot.org/core/title"Elongation factor Ts from Thermus thermophilus -- overproduction in Escherichia coli, quaternary structure and interaction with elongation factor Tu."xsd:string
http://purl.uniprot.org/citations/8617268http://purl.uniprot.org/core/volume"236"xsd:string
http://purl.uniprot.org/citations/8617268http://purl.uniprot.org/core/volume"236"xsd:string
http://purl.uniprot.org/citations/8617268http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8617268
http://purl.uniprot.org/citations/8617268http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8617268