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  • 标题:lsomeric Phenylalanyl-tRNAs. Position of the Aminoacyl Moiety During Protein Biosynthesis
  • 本地全文:下载
  • 作者:Sidney M. Hecht ; John W. Kozarich ; Francis J. Schmidt
  • 期刊名称:Proceedings of the National Academy of Sciences
  • 印刷版ISSN:0027-8424
  • 电子版ISSN:1091-6490
  • 出版年度:1974
  • 卷号:71
  • 期号:11
  • 页码:4317-4321
  • DOI:10.1073/pnas.71.11.4317
  • 语种:English
  • 出版社:The National Academy of Sciences of the United States of America
  • 摘要:The preparation of phenylalanyl-tRNA terminating in 3'-deoxyadenosine has been achieved by incubation of abbreviated tRNA (tRNA-CpCOH) with 3'-deoxyadenosine 5'-diphosphate and polynucleotide phosphorylase (EC 2.7.7.8 ), followed by aminoacylation. The isomeric phenylalanyl-tRNA terminating in 2'-deoxyadenosine was constructed by incubation of tRNA-CpCOH with 2'-deoxy-3'-O-phenylalanyladenosine 5'-diphosphate and polynucleotide phosphorylase. While tRNA is aminoacylated at the 2'-position, only the 3'-aminoacyl-tRNA is active as a peptide acceptor in the peptidyltransferase reaction. Both modified tRNAs were bound to the A-site as efficiently as unmodified tRNA, but neither was so efficient at P-site binding or as an acceptor in the peptidyltransferase reaction. Neither of the modified tRNAs acted as a donor in the peptidyltransferase reaction.
  • 关键词:CTP(ATP):tRNA nucleotidyltransferase ; “chemical” tRNA aminoacylation ; ribosomal binding assays ; peptidyltransferase reaction ; puromycin-like activity
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