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• W1566124273 abstract "Abstract As a part of a more extensive program dealing with the initiation of polypeptide synthesis in cell-free systems of Escherichia coli directed by plant viral RNAs and bacteriophage RNA, the role of N -acetylated aminoacyl-tRNAs in this process has been studied. The viral messenger was RNA derived from the top component a of alfalfa mosaic virus (AMV-RNA). The primary interaction between AMV-RNA and E. coli ribosomes is very selective. Only three species of aminoacyl-tRNA: phenylalanyl-tRNA, isoleucyl-tRNA, and valyl-tRNA can bind to the ribosome-AMV-RNA complex. Two of these species, when N -acetylated, can function as polypeptide chain initiator: N -acetylphenylalanyl-tRNA and N -acetylisoleucyl-tRNA. By contrast N -acetylvalyl-tRNA does not bind to the ribosome-mRNA complex and cannot act as chain initiator either. Analysis of the biosynthetic product formed with N -acetyl- 14 C-phenylalanyl-tRNA revealed that N -acetylphenylalanine is incorporated into the N -terminal structure of the product. Deacetylation appeared to be very limited under the conditions of incorporation. Aminoacyl-tRNA species, which might respond to codons overlapping the two adjacent ones in the hexanucleotide coding for phenylalanine and isoleucine, do not bind to the mRNA-ribosome complex and presumably cannot function as chain initiator when N -acetylated. This has been confirmed experimentally for N -acetylleucyl-tRNA. Ribosomal initiation factors and GTP, which at low Mg 2+ concentration are essential for binding of N -acetylphenylalanyl-tRNA to the ribosomes programmed with poly U, do not promote the binding of the tRNA or N -acetylisoleucyl-tRNA to the AMV-RNA-ribosome complex. It is concluded that chain initiation in the presence of AMV-RNA can occur by means of two different mechanisms: one requires low Mg 2+ concentrations, initiation factors, GTP and N -formylmethionyl-tRNA (F-met-tRNA); the other can make use of N -acetylaminoacyl-tRNAs at relatively high Mg 2+ concentrations in the absence of initiation factors and GTP. The implications in connection with correct translation are discussed." @default.
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• W1566124273 date "1971-07-01" @default.
• W1566124273 modified "2023-09-25" @default.
• W1566124273 title "Chain initiation during polypeptide synthesis in cell-free bacterial systems programmed with a plant viral messenger" @default.
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• W1566124273 doi "https://doi.org/10.1016/0042-6822(71)90114-0" @default.
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