Plant Cell Advance Online Publication
Published on October 11, 2002; 10.1105/tpc.004341
Received May 2, 2002
Accepted August 7, 2002
Proteomic Characterization of the Small Subunit of Chlamydomonas reinhardtii
Chloroplast Ribosome: Identification of a Novel S1 Domain-Containing Protein
and Unusually Large Orthologs of Bacterial S2, S3, and S5
Kenichi Yamaguchi 1, Susana Prieto 1, María Verónica Beligni 1, Paul A. Haynes 2, W. Hayes McDonald 3, John R. Yates III 3, and Stephen P. Mayfield 1*
1
Department of Cell Biology and the Skaggs Institute for Chemical Biology, The Scripps
Research Institute, La Jolla, California 92037
2
Torrey Mesa Research Institute of Syngenta, San Diego, California 92121
3
Department of Cell Biology, The Scripps Research Institute, La Jolla, California
92037
* To whom correspondence should be addressed. E-mail: mayfield{at}scripps.edu.
To understand how chloroplast mRNAs are translated into functional proteins, a detailed
understanding of all of the components of chloroplast translation is needed. To this
end, we performed a proteomic analysis of the plastid ribosomal proteins in the small
subunit of the chloroplast ribosome from the green alga Chlamydomonas reinhardtii
. Twenty proteins were identified, including orthologs of Escherichia coli
S1, S2, S3, S4, S5, S6, S7, S9, S10, S12, S13, S14, S15, S16, S17, S18, S19,
S20, and S21 and a homolog of spinach plastid-specific ribosomal protein-3 (PSRP-3).
In addition, a novel S1 domain-containing protein, PSRP-7, was identified.
Among the identified proteins, S2 (57 kD), S3 (76 kD), and S5 (84 kD) are prominently
larger than their E. coli or spinach counterparts, containing N-terminal
extensions (S2 and S5) or insertion sequence (S3). Structural predictions based on
the crystal structure of the bacterial 30S subunit suggest that the additional domains
of S2, S3, and S5 are located adjacent to each other on the solvent side near the
binding site of the S1 protein. These additional domains may interact with the S1
protein and PSRP-7 to function in aspects of mRNA recognition and translation initiation
that are unique to the Chlamydomonas chloroplast.
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