CHARACTERIZATION OF 3 PROTEINS INVOLVED IN POLYPEPTIDE CHAIN TERMINATION
CHARACTERIZATION OF 3 PROTEINS INVOLVED IN POLYPEPTIDE CHAIN TERMINATION
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DOI:
10.1101/sqb.1969.034.01.053
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发表时间:
1969-01-01
期刊:
影响因子:
--
通讯作者:
KLEIN, HA
中科院分区:
文献类型:
--
作者:
CAPECCHI, MR;KLEIN, HA
At each stage of elongation, the growing polypeptide chain is bound to the ribosome-messenger RNA complex through the transfer RNA of the most recently incorporated amino acid residue (Gilbert, 1963; Bretscher, 1963). When the chain is complete, the last polypeptide-transfer RNA (tRNA) ester linkage is cleaved, releasing the chain from the tRNA and thus from the ribosomal complex. This hydrolysis occurs when the ribosome in the course of moving along the messenger RNA (mRNA) reaches a chain terminating signal. The first step in elucidating the mechanism of polypeptide chain termination was to identify such signals. A purely genetic approach indicated that the codons UAA, UAG, and UGA could act as termination signals (Brenner, Stretton, and Kaplan, 1965; Weigert and Garen, 1965; Sambrook, Fan, and Brenner, 1967; Zipser, 1967). If by mutation such a codon appears, in phase, in the interior of a cistron, premature polypeptide chain termination occurs at the point of genetic alteration (Sarabhai, Stretton, Brenner, and Bolle, 1964). This codon assignment was supported by cell-free studies which showed that random U, A and U, A, G copolymers, unlike the homopolymers, directed the synthesis of polypeptides, some of which were released from the tRNAs (Bretscher, Goodman, Menninger, and Smith, 1965; Takanami and u 1965; Ganoza and Nakamoto, 1966). A more direct confirmation that UAA can trigger polypeptide chain termination was the demonstration that the polyribonucleotide AUGUUUUAAA... directed the synthesis of the released dipeptide N-formylmethionyl (F-met-) phenylalanine (Last, Stanley, Salas, Hille, Wahba and Ochoa, 1967). In order to further decipher the mechanism ofFIOURE I. Outline of the steps required to control the synthesis of the R17 NH2-terminal coat protein hexapeptide, F-met-Ala-Ser-Asn-Phe-14C-Thr, and its release from the ribosomemRNA-pcptidyl tRNA complex. T and R 1 are E. coli factors required for elongation and release of the polypeptide chain respectively.