title: Chloroplast ribosomal protein L15, like L1, L13 and L21, is significantly larger than its E. coli homologue.
abstract: 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.
authors.affiliation: Max-Planck-Institut für Molekulare Genetik, Abteilung Wittmann, Berlin, Germany.
authors.forename: C H
authors.initials: CH
authors.lastname: Johnson
authors.forename: A R
authors.initials: AR
authors.lastname: Subramanian
mesh_terms: 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
chemical_list: D010940:Plant Proteins; D012269:Ribosomal Proteins; C043649:ribosomal protein L15