TEMPLATE-FREE RIBOSOMAL SYNTHESIS OF POLYPEPTIDES FROM AMINOACYL-TRANSFER RNAS
TEMPLATE-FREE RIBOSOMAL SYNTHESIS OF POLYPEPTIDES FROM AMINOACYL-TRANSFER RNAS
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DOI:
10.1016/0303-2647(82)90008-9
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发表时间:
1982-01-01
期刊:
影响因子:
1.6
通讯作者:
SPIRIN, AS
中科院分区:
文献类型:
--
作者:
BELITSINA, NV;TNALINA, GZ;SPIRIN, AS
Escherichia coli ribosomes in the absence of messenger polynucleotides are capable of synthesizing some polypeptides from aminoacyl-tRNA as substrates. EF-Tu induced binding of aminoacyl-tRNA, ribosomal peptidyl transferase and EF-G-promoted translocation are strictly required for this template-free elongation. Typical ribosomal inhibitors such as tetracycline, chloramphenicol, phenylboric acid and fusidic acid inhibit the template-free synthesis of polypeptides. The synthesis requires GTP cleavage; a non-cleavable analog of GTP, guanyl-5''-yl methylenediphosphonate does not maintain the synthesis. Among 16 different aminoacyl-tRNA studied as substrates for the ribosomal template-free synthesis of polypeptides Lys-tRNA, Ser-tRNA, Thr-tRNA and Asp-tRNA were the best. Gly-tRNA, Glu-tRNA, Val-tRNA, Arg-tRNA, Ala-tRNA and Leu-tRNA as substrates gave relatively low levels of the polypeptide synthesis on non-programmed ribosomes. Pro-tRNA, Phe-tRNA, Asn-tRNA, Met-tRNA, Ile-tRNA and Gln-tRNA were practically inactive as substrates for the template-free elongation. No correlation was found between the abilities of the aminoacyl-tRNA to serve as substrates for the template-free elongation and their activities in template-free binding to ribosomes.