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. 1982 Nov;79(22):6871-5.
doi: 10.1073/pnas.79.22.6871.

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

M Bartsch  1 , M Kimura, A R Subramanian
Affiliations

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

M Bartsch et al. Proc Natl Acad Sci U S A. 1982 Nov.

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%).

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