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. 1982 Nov;79(22):6871–6875. doi: 10.1073/pnas.79.22.6871

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

Marius Bartsch 1, Makoto Kimura 1, Alap-Raman Subramanian 1,*
PMCID: PMC347235  PMID: 16593249

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 Mr 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 NH2-terminal region (<20%).

Keywords: amino acid sequence, protein evolution, organelle ribosome, acidic L7, L12 protein, Spinacia oleracea

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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