Role of GTP in the Positioning of Formylmethionyl-tRNAf on the E. coli Ribosome

FORMATION of the E. coli initiation complex between ribosomal subunits, natural messenger RNA and formyl-methionyl-tRNA f (fMet-tRNA f ) requires the presence of initiation factors and GTP 1–3 . In the binding reaction, GTP can be replaced by an analogue, guanylyl-5′-methylene-diphosphonate (GMP-PCP...

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Veröffentlicht in:	Nature. New biology (London) 1971-12, Vol.234 (50), p.216-218
1. Verfasser:	KUECHLER, ERNST
Format:	Artikel
Sprache:	eng
Schlagworte:	Binding Sites Biomedical and Life Sciences Electrophoresis Electrophoresis, Paper Escherichia coli - drug effects Escherichia coli - metabolism Formates - metabolism Genetic Code Guanosine Triphosphate - pharmacology letters-to-editor Life Sciences Methionine - metabolism Peptide Biosynthesis Peptide Chain Initiation, Translational Protein Binding Ribonucleases Ribosomes - drug effects Ribosomes - metabolism RNA, Bacterial - metabolism RNA, Transfer - metabolism Sulfur Isotopes
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Beschreibung
Zusammenfassung:	FORMATION of the E. coli initiation complex between ribosomal subunits, natural messenger RNA and formyl-methionyl-tRNA f (fMet-tRNA f ) requires the presence of initiation factors and GTP 1–3 . In the binding reaction, GTP can be replaced by an analogue, guanylyl-5′-methylene-diphosphonate (GMP-PCP), but the complex does not then react with puro-mycin. Hydrolysis of GTP is therefore required for the formation of an active initiation complex able to carry out peptide bond formation 4 .
ISSN:	0090-0028 2058-1092
DOI:	10.1038/newbio234216a0