First published online February 25, 2005; 10.1104/pp.104.053637
Plant Physiology 137:848-862 (2005)
© 2005 American Society of Plant Biologists
BIOCHEMICAL PROCESSES AND MACROMOLECULAR STRUCTURES
Proteomic Characterization of Evolutionarily Conserved and Variable Proteins of Arabidopsis Cytosolic Ribosomes1,[w]
Ing-Feng Chang2,
Kathleen Szick-Miranda2,
Songqin Pan and
Julia Bailey-Serres*
Center for Plant Cell Biology, Department of Botany and Plant Sciences, University of California, Riverside, California 92521–0124 (I.-F.C., S.P., J.B.-S.); and Department of Biology, California State University, Bakersfield, California 93311 (K.S.-M.)
Analysis of 80S ribosomes of Arabidopsis (Arabidopsis thaliana) by use of high-speed centrifugation, sucrose gradient fractionation, one- and two-dimensional gel electrophoresis, liquid chromatography purification, and mass spectrometry (matrix-assisted laser desorption/ionization time-of-flight and electrospray ionization) identified 74 ribosomal proteins (r-proteins), of which 73 are orthologs of rat r-proteins and one is the plant-specific r-protein P3. Thirty small (40S) subunit and 44 large (60S) subunit r-proteins were confirmed. In addition, an ortholog of the mammalian receptor for activated protein kinase C, a tryptophan-aspartic acid-domain repeat protein, was found to be associated with the 40S subunit and polysomes. Based on the prediction that each r-protein is present in a single copy, the mass of the Arabidopsis 80S ribosome was estimated as 3.2 MD (1,159 kD 40S; 2,010 kD 60S), with the 4 single-copy rRNAs (18S, 26S, 5.8S, and 5S) contributing 53% of the mass. Despite strong evolutionary conservation in r-protein composition among eukaryotes, Arabidopsis 80S ribosomes are variable in composition due to distinctions in mass or charge of approximately 25% of the r-proteins. This is a consequence of amino acid sequence divergence within r-protein gene families and posttranslational modification of individual r-proteins (e.g. amino-terminal acetylation, phosphorylation). For example, distinct types of r-proteins S15a and P2 accumulate in ribosomes due to evolutionarily divergence of r-protein genes. Ribosome variation is also due to amino acid sequence divergence and differential phosphorylation of the carboxy terminus of r-protein S6. The role of ribosome heterogeneity in differential mRNA translation is discussed.
1 This research was supported by the National Science Foundation (grant no. DBI 021187 to J.B.-S.), by the U.S. Department of Agriculture (grant no. 00–35301–9108 to J.B.-S.), and by the Ministry of Education, Republic of China, Taiwan (grant to I.-F.C.).
2 These authors contributed equally to the paper.
[w] The online version of this article contains Web-only data.
Article, publication date, and citation information can be found at www.plantphysiol.org/cgi/doi/10.1104/pp.104.053637.
* Corresponding author; e-mail serres{at}ucr.edu; fax 951–827–4437.
Received September 16, 2004;
returned for revision November 16, 2004;
accepted November 23, 2004.
This article has been cited by other articles:
|
|
|
|
 
J. Guo, J. Wang, L. Xi, W.-D. Huang, J. Liang, and J.-G. Chen
RACK1 is a negative regulator of ABA responses in Arabidopsis
J. Exp. Bot.,
September 1, 2009;
60(13):
3819 - 3833.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
J. Guo, S. Wang, J. Wang, W.-D. Huang, J. Liang, and J.-G. Chen
Dissection of the Relationship Between RACK1 and Heterotrimeric G-Proteins in Arabidopsis
Plant Cell Physiol.,
September 1, 2009;
50(9):
1681 - 1694.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
C. A. Whittle and J. E. Krochko
Transcript Profiling Provides Evidence of Functional Divergence and Expression Networks among Ribosomal Protein Gene Paralogs in Brassica napus
PLANT CELL,
August 1, 2009;
21(8):
2203 - 2219.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
A. Nakashima, L. Chen, N. P. Thao, M. Fujiwara, H. L. Wong, M. Kuwano, K. Umemura, K. Shirasu, T. Kawasaki, and K. Shimamoto
RACK1 Functions in Rice Innate Immunity by Interacting with the Rac1 Immune Complex
PLANT CELL,
August 1, 2008;
20(8):
2265 - 2279.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
M. Ueda, T. Nishikawa, M. Fujimoto, H. Takanashi, S.-i. Arimura, N. Tsutsumi, and K.-i. Kadowaki
Substitution of the Gene for Chloroplast RPS16 Was Assisted by Generation of a Dual Targeting Signal
Mol. Biol. Evol.,
August 1, 2008;
25(8):
1566 - 1575.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
R. F. Degenhardt and P. C. Bonham-Smith
Arabidopsis Ribosomal Proteins RPL23aA and RPL23aB Are Differentially Targeted to the Nucleolus and Are Disparately Required for Normal Development
Plant Physiology,
May 1, 2008;
147(1):
128 - 142.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
A. J. Carroll, J. L. Heazlewood, J. Ito, and A. H. Millar
Analysis of the Arabidopsis Cytosolic Ribosome Proteome Provides Detailed Insights into Its Components and Their Post-translational Modification
Mol. Cell. Proteomics,
February 1, 2008;
7(2):
347 - 369.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
J.-G. Chen, H. Ullah, B. Temple, J. Liang, J. Guo, J. M. Alonso, J. R. Ecker, and A. M. Jones
RACK1 mediates multiple hormone responsiveness and developmental processes in Arabidopsis
J. Exp. Bot.,
August 1, 2006;
57(11):
2697 - 2708.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
S. Baginsky and W. Gruissem
Arabidopsis thaliana proteomics: from proteome to genome
J. Exp. Bot.,
April 1, 2006;
57(7):
1485 - 1491.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
M. E. Zanetti, I.-F. Chang, F. Gong, D. W. Galbraith, and J. Bailey-Serres
Immunopurification of Polyribosomal Complexes of Arabidopsis for Global Analysis of Gene Expression
Plant Physiology,
June 1, 2005;
138(2):
624 - 635.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
