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：1973
卷号：70
期号：10
页码：2874-2878
DOI：10.1073/pnas.70.10.2874
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：An inhibitor of polypeptide-chain initiation was isolated from E. coli cells. This protein inhibits formation of the 30S or 70S initiation complex with either fMet-tRNAf as initiator and AUG, MS2 RNA, or late T4 RNA as messenger, or acPhe-tRNA as initiator and poly(U) as messenger. Chain elongation, e.g., poly(U) translation at high Mg2+ concentration, is not inhibited. The inhibitor is rendered ineffective when active aminoacylation of tRNA is taking place, e.g., during natural mRNA translation. This inhibitor is distinct from the so-called interference (i) factors, which interfere exclusively with the action of initiation factor 3. Since the new inhibitor can apparently be turned on and off, it may have a regulatory function in translation.
