Johnson C H, Subramanian A R
Max-Planck-Institut für Molekulare Genetik, Abteilung Wittmann, Berlin, Germany.
FEBS Lett. 1991 May 6;282(2):268-72. doi: 10.1016/0014-5793(91)80492-l.
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.
