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Structure,mechanism and evolution of chloroplast transfer RNA processing systems
Authors:Peter Gegenheimer
Institution:(1) Departments of Biochemistry and of Botany, and Molecular Genetics Program, The University of Kansas, 2045 Haworth Hall, 66045-2106 Lawrence, KS, USA
Abstract:Chloroplasts of land plants have an active transfer RNA processing system, consisting of an RNase P-like 5prime endonuclease, a 3prime endonuclease, and a tRNA:CCA nucleotidyltransferase. The specificity of these enzymes resembles more that of their eukaryotic counterparts than that of their cyanobacterial predecessors. Most strikingly, chloroplast RNase P activity almost certainly resides in a protein, rather than in an RNA protein complex as in Bacteria, Archaea, and Eukarya. The chloroplast enzyme may have evolved from a preexisting chloroplast NADP-binding protein. Chloroplast RNase P cleaves pre-tRNA by a reaction mechanism in which at least one of the Mg2+ ions utilized by the bacterial ribozyme RNase P is replaced by an amino acid side chain.Abbreviations pre-tRNA precursor to tRNA - pCp cytidine 5prime, 3prime-bisphosphate - IC50 inhibitor concentration giving 50% inhibition - GAPDH glyceraldehyde 3-phosphate dehydrogenase
Keywords:catalytic mechanism  endonuclease  magnesium  NADPH  pathway  protein  RNase P
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