Chloroplast ribosomal protein L15, like L1, L13 and L21, is significantly larger than its E. coli homologue

FEBS Letters

Subramanian, Alap R.¹  Johnson, Clayton H.¹ 

[1] Max-Planck-Institut für Molekulare Genetik, Abteilung Wittmann, Ihnestrasse 73, W-1000 Berlin 33, Germany

关键词: Chloroplast ribosome;    Ribosomal protein L15;    Chloroplast-bacterial immunohomology;    Spinach;    Spinacia oleracea;    r-protein;    ribosomal protein;    PAGE;    polyacrylamide gel electrophoresis;    PBS;    phosphate buffered saline (10 mM NaH2PO4;    pH 7.2;    150 mM NaCl);    L-proteins;    large ribosomal subunit proteins;   

DOI  :  10.1016/0014-5793(91)80492-L

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The purification and identification by peptide sequence and immunological data of spinach chloroplast homologue of E. coli L15 is presented. A signification 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

【 授权许可】

Unknown