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PMID: 16593249 Published · ppublish English Journal Article

Purification, primary structure, and homology relationships of a chloroplast ribosomal protein.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 79 ·No. 22 ·1982-11-00 ·Pages 6871-5

Bartsch M, Kimura M, Subramanian AR

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%).

Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Bartsch M
Max-Planck-Institut für Molekulare Genetik, Abteilung Wittmann, Ihnestrasse 63-73, D-1000 Berlin 33, Germany.
Kimura M
Subramanian A R
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.79.22.6871
Published
1982-11-00
Pages
6871-5
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC347235
External Links
PubMed source DOI: 10.1073/pnas.79.22.6871 PMC Full Text View journal details
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