Abstract
A chloroplast ribosomal protein that showed immunological homology to Escherichia coli ribosomal protein L12 was purified from spinach ( Spinacia oleracea ) leaves and its primary structure was determined by manual micro Edman degradation. The protein is composed of 130 amino acid residues and has M r 13,576. It shows structural features characteristic of the L12 proteins of eubacterial 70S ribosomes (e.g., identical amino acid residues in about 50% of the sequence) but no apparent homology to the L12-type proteins of eukaryotic cytoplasmic 80S ribosomes. The homology to eubacterial proteins is highest in the COOH-terminal region (70%) and low in the NH 2 -terminal region (<20%).
Dates
Type | When |
---|---|
Created | 19 years, 2 months ago (May 31, 2006, 4:58 a.m.) |
Deposited | 3 years, 4 months ago (April 13, 2022, 12:01 p.m.) |
Indexed | 1 year, 9 months ago (Nov. 23, 2023, 1:08 a.m.) |
Issued | 42 years, 9 months ago (Nov. 1, 1982) |
Published | 42 years, 9 months ago (Nov. 1, 1982) |
Published Online | 42 years, 9 months ago (Nov. 1, 1982) |
Published Print | 42 years, 9 months ago (Nov. 1, 1982) |
@article{Bartsch_1982, title={Purification, primary structure, and homology relationships of a chloroplast ribosomal protein}, volume={79}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.79.22.6871}, DOI={10.1073/pnas.79.22.6871}, number={22}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Bartsch, Marius and Kimura, Makoto and Subramanian, Alap-Raman}, year={1982}, month=nov, pages={6871–6875} }