TAILIEUCHUNG - Báo cáo khoa học: Proteomic identification of all plastid-specific ribosomal proteins in higher plant chloroplast 30S ribosomal subunit PSRP-2 (U1A-type domains), PSRP-3a/b (ycf65 homologue) and PSRP-4 (Thx homologue)

Six ribosomal proteins are specific to higher plant chloro-plast ribosomes [Subramanian,. (1993)TrendsBiochem. , 177–180]. Three of them have been fully character-ized [Yamaguchi, K., von Knoblauch, K. & Subramanian, A. R. (2000) J. Biol. , 28455–28465; Yamaguchi, K. &Subramanian, A. R. (2000) J. Biol. , 28466– 28482]. The remaining three plastid-specific ribosomal pro-teins (PSRPs), all on the small subunit, have now been characterized (2D PAGE, HPLC,N-terminal/internal pep-tide sequencing, electrospray ionization MS, cloning/ sequencing of precursor cDNAs). . | Eur. J. Biochem. 270 190-205 2003 FEBS 2003 doi Proteomic identification of all plastid-specific ribosomal proteins in higher plant chloroplast 30S ribosomal subunit PSRP-2 U1A-type domains PSRP-3a p ycf65 homologue and PSRP-4 Thx homologue Kenichi Yamaguchi and Alap R. Subramanian Max-Planck-Institut fuer molekulare Genetik Berlin-Dahlem Germany and Department of Biochemistry University of Arizona Tucson USA Six ribosomal proteins are specific to higher plant chloroplast ribosomes Subramanian . 1993 TrendsBiochem. Sci. 18 177-180 . Three of them have been fully characterized Yamaguchi K. von Knoblauch K. Subramanian A. R. 2000 J. Biol. Chem. 275 28455-28465 Yamaguchi K. Subramanian A. R. 2000 J. Biol. Chem. 275 2846628482 . The remaining three plastid-specific ribosomal proteins PSRPs all on the small subunit have now been characterized 2D PAGE HPLC N-terminal internal peptide sequencing electrospray ionization MS cloning sequencing of precursor cDNAs . PSRP-3 exists in two forms a b N-terminus free and blocked by post-translational modification whereas PSRP-2 and PSRP-4 appear from MS data to be unmodified. PSRP-2 contains two RNA-binding domains which occur in mRNA processing stabilizing proteins . U1A snRNP poly A -binding proteins suggesting a possible role for it in the recruiting of stored chloroplast mRNAs for active protein synthesis. PSRP-3 is the higher plant orthologue of a hypothetical protein ycf65 gene product first reported in the chloroplast genome of a red alga. The ycf65 gene is absent from the chloroplast genomes of higher plants. Therefore we suggest that Psrp-3Ịycf65 encoding an evolutionarily conserved chloroplast ribosomal protein represents an example of organelle-to-nucleus gene transfer in chloroplast evolution. PSRP-4 shows strong homology with Thx a small basic ribosomal protein of Thermus thermophilus 30S subunit with a specific structural role in the subunit crystallographic structure but its .

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