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• W1573582959 abstract "This chapter discusses the essential features of ribosome-catalyzed peptide-bond formation and the involvement of ribosomal ribonucleic acid (rRNA) in the catalysis of this critical reaction. Peptide-bond formation, the covalent linkage of amino acids during messenger RNA (mRNA) translation, is among the most fundamental biochemical transformations in nature and is the principal catalytic activity of ribosomes. Ribosomes are complex ribonucleoprotein (RNP) particles, comprising in all organisms of two subunits; in the eubacterium Escherichia coli, the 30-S ribosomal subunit is composed of 16-S rRNA and a single copy each of 21 ribosomal proteins, whereas the 50-S ribosomal subunit consists of 5-S rRNA, 23-S rRNA, and 32 different proteins, one of which is present in four copies. Translation of mRNA is initiated, by the assembly of a ternary coniplex, between the 30-5 subunit, mRNA, and the initiation-specific aminoacyl tRNA (aa-tRNA) substrate, fMet-tRNAfMet. However, the ribosome is a processive enzyme; thus, following the peptide-bond formation, a translocation event occurs, in which the movement of tRNA substrates and mRNA is promoted, by interaction with another GTPase elongation factor G." @default.
• W1573582959 created "2016-06-24" @default.
• W1573582959 creator A5028628444 @default.
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• W1573582959 date "1995-01-01" @default.
• W1573582959 modified "2023-09-25" @default.
• W1573582959 title "Ribosome-catalyzed Pep tide-bond Formation" @default.
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• W1573582959 doi "https://doi.org/10.1016/s0079-6603(08)60809-0" @default.
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