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Title: Chloroplast ribosomal protein L15, like L1, L13 and L21, is significantly larger than its E. coli homologue. Author: Johnson CH, Subramanian AR. Journal: FEBS Lett; 1991 May 06; 282(2):268-72. PubMed ID: 2037044. 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.[Abstract] [Full Text] [Related] [New Search]