{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2024,6,21]],"date-time":"2024-06-21T09:05:51Z","timestamp":1718960751928},"reference-count":37,"publisher":"American Society for Microbiology","issue":"2","license":[{"start":{"date-parts":[[1979,11,1]],"date-time":"1979-11-01T00:00:00Z","timestamp":310262400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Bacteriol"],"published-print":{"date-parts":[[1979,11]]},"abstract":"<jats:p>\n            To elucidate subtle functions of transfer ribonucleic acid (tRNA) modifications in protein synthesis, pairs of tRNA's that differ in modifications at specific positions were prepared from\n            <jats:italic>Bacillus subtilis<\/jats:italic>\n            . The tRNA's differ in modifications in the anticodon loop, the extra arm, and the T C loop. The functional properties of these species were compared in aminoacylation, as well as in initiation and peptide bond formation, at programmed ribosomes. These experiments demonstrated the following. (i) In tRNA\n            <jats:sub>f<\/jats:sub>\n            <jats:sup>Met<\/jats:sup>\n            the methylation of guanosine 46 in the extra arm to 7-methylguanosine by the 7-methylguanosine\u2013forming enzyme from\n            <jats:italic>Escherichia coli<\/jats:italic>\n            changes the aminoacylation kinetics for the\n            <jats:italic>B. subtilis<\/jats:italic>\n            methionyl-tRNA synthetase. In repeated experiments the\n            <jats:italic>V<\/jats:italic>\n            <jats:sub>max<\/jats:sub>\n            value is decreased by one-half. (ii) tRNA\n            <jats:sub>f<\/jats:sub>\n            <jats:sup>Met<\/jats:sup>\n            species with ribothymidine at position 54 (rT54) or uridine at position 54 (U54) were obtained from untreated or trimethoprim-treated\n            <jats:italic>B. subtilis<\/jats:italic>\n            . The formylated fMet-tRNA\n            <jats:sub>f<\/jats:sub>\n            <jats:sup>Met<\/jats:sup>\n            species with U54 and rT54, respectively, function equally well in an in vitro initiation system containing AUG, initiation factors, and 70s ribosomes. The unformylated Met-tRNA\n            <jats:sub>t<\/jats:sub>\n            <jats:sup>Met<\/jats:sup>\n            species, however, differ from each other: \u201cMet-tRNA\n            <jats:sub>f<\/jats:sub>\n            <jats:sup>Met<\/jats:sup>\n            rT\u201d is inactive, whereas the U54 counter-upart effectively forms the initiation complex. (iii) Two isoacceptors, tRNA\n            <jats:sub>1<\/jats:sub>\n            <jats:sup>Phe<\/jats:sup>\n            and tRNA\n            <jats:sub>2<\/jats:sub>\n            <jats:sup>Phe<\/jats:sup>\n            , were obtained from\n            <jats:italic>B. subtilis<\/jats:italic>\n            . tRNA\n            <jats:sub>1<\/jats:sub>\n            <jats:sup>Phe<\/jats:sup>\n            accumulates only under special growth conditions and is an incompletely modified precursor oftRNA\n            <jats:sub>2<\/jats:sub>\n            <jats:sup>Phe<\/jats:sup>\n            : in the first position of the anticodon, guanosine replaces Gm, and next to the 3\u2032 end of the anticodon (isopentenyl)adenosine replaces 2-thiomethyl-\n            <jats:italic>N<\/jats:italic>\n            <jats:sup>6<\/jats:sup>\n            -(isopentenyl)adenosine. Both tRNA's behave identically in aminoacylation kinetics. In the factor-dependent AUGU\n            <jats:sub>3<\/jats:sub>\n            -directed formation of fMet-Phe, the undermodified tRNA\n            <jats:sub>1<\/jats:sub>\n            <jats:sup>Phe<\/jats:sup>\n            is always less efficient at Mg\n            <jats:sup>2+<\/jats:sup>\n            concentrations between 5 and 15 mM than its mature counterpart.\n          <\/jats:p>","DOI":"10.1128\/jb.140.2.408-414.1979","type":"journal-article","created":{"date-parts":[[2020,1,3]],"date-time":"2020-01-03T16:56:40Z","timestamp":1578070600000},"page":"408-414","update-policy":"http:\/\/dx.doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":16,"title":["Function of Modified Nucleosides 7-Methylguanosine, Ribothymidine, and 2-Thiomethyl-\n            <i>N<\/i>\n            <sup>6<\/sup>\n            -(Isopentenyl)adenosine in Procaryotic Transfer Ribonucleic Acid"],"prefix":"10.1128","volume":"140","author":[{"given":"A.","family":"Hoburg","sequence":"first","affiliation":[{"name":"Institut f\u00fcr Physiologische Chemie der Universit\u00e4t Erlangen-N\u00fcrnberg, 8520 Erlangen, Federal Republic of Germany"}]},{"given":"H. J.","family":"Aschhoff","sequence":"additional","affiliation":[{"name":"Institut f\u00fcr Physiologische Chemie der Universit\u00e4t Erlangen-N\u00fcrnberg, 8520 Erlangen, Federal Republic of Germany"}]},{"given":"H.","family":"Kersten","sequence":"additional","affiliation":[{"name":"Institut f\u00fcr Physiologische Chemie der Universit\u00e4t Erlangen-N\u00fcrnberg, 8520 Erlangen, Federal Republic of Germany"}]},{"given":"U.","family":"Manderschied","sequence":"additional","affiliation":[{"name":"Institut f\u00fcr Organische Chemie und Biochemie Technische Hochschule Darmstadt, 6100 Darmstadt, Federal Republic of Germany"}]},{"given":"H. G.","family":"Gassen","sequence":"additional","affiliation":[{"name":"Institut f\u00fcr Organische Chemie und Biochemie Technische Hochschule Darmstadt, 6100 Darmstadt, Federal Republic of Germany"}]}],"member":"235","reference":[{"key":"p_1","doi-asserted-by":"crossref","unstructured":"Agris P. F. and D. Soll. 1977. 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