Open AccessA Specific Inhibitor of Polypeptide-Chain Initiation in Escherichia coli
Author(s) -
Sylvia LeeHuang,
Henry Lee,
Severo Ochoa
Publication year - 1973
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.70.10.2874
Subject(s) - translation (biology) , messenger rna , aminoacylation , protein biosynthesis , eukaryotic translation , transfer rna , rna , five prime cap , biology , biochemistry , chemistry , microbiology and biotechnology , rna editing , gene
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-tRNA(f) 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 Mg(2+) 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.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom