PMID:7592851
| Citation |
Ganoza, MC, Cunningham, C and Green, RM (1995) A new factor from Escherichia coli affects translocation of mRNA. J. Biol. Chem. 270:26377-81 |
|---|---|
| Abstract |
Reconstitution of protein synthesis from purified translation factors on ribosomes from Escherichia coli has revealed the requirement for a protein, W, that affects chain elongation and is essential to reconstitute the process (Ganoza, M. C., Cunningham, C., and Green, R. M. (1985) Proc. Natl. Acad. Sci. U.S.A. 82, 1648-1652). We report that W has no effect on initiation complex formation by 30 or 70 S ribosomes or on the association of ribosomal subunits, peptide bond synthesis, or binding Ala-tRNA, which is the second amino acid of the coat protein of the MS2 RNA virion. W has a pronounced effect on tripeptide synthesis, and is obligatory for the synthesis of the coat protein or of the hexapeptide encoded by f2am3 RNA. Extracts from a temperature-sensitive mutant of the translocase, EF-G, were purified free of the W protein and were used to score for translocation defects. W is required for binding Ser-tRNA, the third N-terminal amino acid of the MS2 or f2 RNA coat protein to ribosomes bearing fMet-Ala-tRNA, as well as for the ejection of deacyl-tRNA from ribosomes, which occurred concomitant with the binding of the Ser-tRNA. We propose that W functions by ejecting tRNAs from ribosomes in a step that precedes the movement of mRNA during translocation. |
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| Keywords |
Bacterial Proteins/isolation & purification; Bacterial Proteins/metabolism; Capsid/biosynthesis; Escherichia coli/genetics; Escherichia coli/metabolism; GTP Phosphohydrolase-Linked Elongation Factors/metabolism; Kinetics; Levivirus/metabolism; Peptide Elongation Factor G; Peptide Elongation Factors/isolation & purification; Peptide Elongation Factors/metabolism; Protein Biosynthesis; RNA, Messenger/metabolism; RNA, Transfer, Ala/metabolism; RNA, Transfer, Amino Acid-Specific/metabolism; RNA, Transfer, Ser/metabolism; Ribosomes/metabolism; Virion/metabolism |
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