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Biochem Soc Trans ; 38(2): 422-7, 2010 Apr.
Article in English | MEDLINE | ID: mdl-20298195

ABSTRACT

Structural analysis, supported by biochemical, mutagenesis and computational evidence, indicates that the peptidyltransferase centre of the contemporary ribosome is a universal symmetrical pocket composed solely of rRNA. This pocket seems to be a relic of the proto-ribosome, an ancient ribozyme, which was a dimeric RNA assembly formed from self-folded RNA chains of identical, similar or different sequences. This could have occurred spontaneously by gene duplication or gene fusion. This pocket-like entity was capable of autonomously catalysing various reactions, including peptide bond formation and non-coded or semi-coded amino acid polymerization. Efforts toward the structural definition of the early entity capable of genetic decoding involve the crystallization of the small ribosomal subunit of a bacterial organism harbouring a single functional rRNA operon.


Subject(s)
RNA, Catalytic/genetics , RNA, Catalytic/physiology , Ribosomes/genetics , Ribosomes/physiology , Evolution, Molecular , Models, Biological , Models, Molecular , Nucleic Acid Conformation , Protein Binding , Protein Biosynthesis/physiology , RNA, Catalytic/chemistry , RNA, Catalytic/metabolism , Ribosome Subunits, Large, Bacterial/chemistry , Ribosome Subunits, Large, Bacterial/metabolism , Ribosome Subunits, Small, Bacterial/chemistry , Ribosome Subunits, Small, Bacterial/metabolism , Ribosome Subunits, Small, Bacterial/ultrastructure , Ribosomes/metabolism
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