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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Control of Arginine Biosynthesis in <italic>Escherichia coli</italic>: Characterization of Arginyl-Transfer Ribonucleic Acid Synthetase Mutants</title><author><name sortKey="Williams, A L" sort="Williams, A L" uniqKey="Williams A" first="A. L." last="Williams">A. L. Williams</name></author><author><name sortKey="Williams, L S" sort="Williams, L S" uniqKey="Williams L" first="L. S." last="Williams">L. S. Williams</name></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">4570786</idno><idno type="pmc">251714</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC251714</idno><idno type="RBID">PMC:251714</idno><date when="1973">1973</date><idno type="wicri:Area/Pmc/Corpus">000048</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000048</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Control of Arginine Biosynthesis in <italic>Escherichia coli</italic>: Characterization of Arginyl-Transfer Ribonucleic Acid Synthetase Mutants</title><author><name sortKey="Williams, A L" sort="Williams, A L" uniqKey="Williams A" first="A. L." last="Williams">A. L. Williams</name></author><author><name sortKey="Williams, L S" sort="Williams, L S" uniqKey="Williams L" first="L. S." last="Williams">L. S. Williams</name></author></analytic><series><title level="j">Journal of Bacteriology</title><idno type="ISSN">0021-9193</idno><idno type="eISSN">1098-5530</idno><imprint><date when="1973">1973</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>The arginyl-transfer ribonucleic acid (Arg-tRNA) synthetase (EC 6.1.1.13, arginine: RNA ligase adenosine monophosphate) mutants, exhibiting nonrepressible synthesis of arginine by exogenous arginine, were employed in studies of several biochemical properties. Two of these mutants possessed Arg-tRNA synthetases with a reduced affinity for arginine, and this enzyme of another mutant had a reduced affinity for arginine-tRNA (tRNA<sup>arg</sup>). The mutant possessing an Arg-tRNA synthetase with an altered <italic>K<sub>m</sub></italic> for tRNA<sup>arg</sup> was found to have reduced in vivo aminoacylation of two of the five isoaccepting species of tRNA<sup>arg</sup> and complete absence of aminoacylation of one of the isoaccepting species.</p></div></front></TEI><pmc article-type="research-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<front><journal-meta><journal-id journal-id-type="nlm-ta">J Bacteriol</journal-id><journal-title>Journal of Bacteriology</journal-title><issn pub-type="ppub">0021-9193</issn><issn pub-type="epub">1098-5530</issn></journal-meta><article-meta><article-id pub-id-type="pmid">4570786</article-id><article-id pub-id-type="pmc">251714</article-id><article-categories><subj-group subj-group-type="heading"><subject>Genetics and Molecular Biology</subject></subj-group></article-categories><title-group><article-title>Control of Arginine Biosynthesis in <italic>Escherichia coli</italic>: Characterization of Arginyl-Transfer Ribonucleic Acid Synthetase Mutants</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Williams</surname><given-names>A. L.</given-names></name></contrib><contrib contrib-type="author"><name><surname>Williams</surname><given-names>L. S.</given-names></name></contrib></contrib-group><aff id="af1">Department of Biological Sciences, Purdue University, Lafayette, Indiana 47907</aff><pub-date pub-type="ppub"><month>03</month><year>1973</year></pub-date><volume>113</volume><issue>3</issue><fpage>1433</fpage><lpage>1441</lpage><copyright-statement>Copyright © 1973 American Society for Microbiology</copyright-statement><abstract><p>The arginyl-transfer ribonucleic acid (Arg-tRNA) synthetase (EC 6.1.1.13, arginine: RNA ligase adenosine monophosphate) mutants, exhibiting nonrepressible synthesis of arginine by exogenous arginine, were employed in studies of several biochemical properties. Two of these mutants possessed Arg-tRNA synthetases with a reduced affinity for arginine, and this enzyme of another mutant had a reduced affinity for arginine-tRNA (tRNA<sup>arg</sup>). The mutant possessing an Arg-tRNA synthetase with an altered <italic>K<sub>m</sub></italic> for tRNA<sup>arg</sup> was found to have reduced in vivo aminoacylation of two of the five isoaccepting species of tRNA<sup>arg</sup> and complete absence of aminoacylation of one of the isoaccepting species.</p></abstract></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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