Chloroplast ribosomal protein L15, like L1, L13 and L21, is significantly larger than its E. coli homologue.
The purification and identification by peptide sequence and immunological data of the spinach chloroplast homologue of E. coli L15 is presented. A significant increase in its mass over the E. coli counterpart is shown and is accounted for, in part, by a sequenced 18-residue N-terminal extension. A still larger C-terminal extension or internal insertion(s) is inferred. The migration position of the L15 in a 2D gel pattern of spinach chloroplast 50S subunit proteins is shown. Lack of sequence identity with the known chloroplast genomic data confirms the nuclear coding of this protein, and the N-terminal sequence given here provides the transit peptide cleavage site of the cytoplasmic precursor.
Johnson
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CH
Max-Planck-Institut für Molekulare Genetik, Abteilung Wittmann, Berlin, Germany.
Subramanian
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AR
D000595:Amino Acid Sequence; D015153:Blotting, Western; D002736:Chloroplasts / Q000737:chemistry*; D003429:Cross Reactions; D015180:Electrophoresis, Gel, Two-Dimensional; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010940:Plant Proteins / Q000737:chemistry*; D012269:Ribosomal Proteins / Q000737:chemistry* / Q000276:immunology
D010940:Plant Proteins; D012269:Ribosomal Proteins; C043649:ribosomal protein L15