Plant Physiology Preview
Published on November 24, 2004; 10.1104/pp.104.053835
Received September 21, 2004
Returned for revision October 7, 2004
Accepted October 9, 2004
Inactivation of the clpC1 Gene Encoding a Chloroplast Hsp100 Molecular Chaperone Causes Growth Retardation, Leaf Chlorosis, Lower Photosynthetic Activity, and a Specific Reduction in Photosystem Content
Lars L.E. Sjögren , Tara M. MacDonald , Sirkka Sutinen , and Adrian K. Clarke *
Botanical Institute, Göteborg University, SE-405 30 Göteborg, Sweden
The Finnish Forest Research Institute, Joensuu Research Center, Fin-801 01, Finland
* Corresponding author; email: adrian.clarke{at}botany.gu.se.
ClpC is a molecular chaperone of the Hsp100 family. In higher plants there are two chloroplast-localized paralogs (ClpC1 and ClpC2) that are approximately 93% similar in primary sequence. In this study, we have characterized two independent Arabidopsis (Arabidopsis thaliana) clpC1 T-DNA insertion mutants lacking on average 65% of total ClpC content. Both mutants display a retarded-growth phenotype, leaves with a homogenous chlorotic appearance throughout all developmental stages, and more perpendicular secondary influorescences. Photosynthetic performance was also impaired in both knockout lines, with relatively fewer photosystem I and photosystem II complexes, but no changes in ATPase and Rubisco content. However, despite the specific drop in photosystem I and photosystem II content, no changes in leaf cell anatomy or chloroplast ultrastructure were observed in the mutants compared to the wild type. Previously proposed functions for envelope-associated ClpC in chloroplast protein import and degradation of mistargeted precursors were examined and shown not to be significantly impaired in the clpC1 mutants. In the stroma, where the majority of ClpC protein is localized, marked increases of all ClpP paralogs were observed in the clpC1 mutants but less variation for the ClpR paralogs and a corresponding decrease in the other chloroplast-localized Hsp100 protein, ClpD. Increased amounts of other stromal molecular chaperones (Cpn60, Hsp70, and Hsp90) and several RNA-binding proteins were also observed. Our data suggest that overall ClpC as a stromal molecular chaperone plays a vital role in chloroplast function and leaf development and is likely involved in photosystem biogenesis.
This article has been cited by other articles:
|
|
|
|
 
T. Ogawa, K. Nishimura, T. Aoki, H. Takase, K.-I. Tomizawa, H. Ashida, and A. Yokota
A Phosphofructokinase B-Type Carbohydrate Kinase Family Protein, NARA5, for Massive Expressions of Plastid-Encoded Photosynthetic Genes in Arabidopsis
Plant Physiology,
September 1, 2009;
151(1):
114 - 128.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
B. Zybailov, G. Friso, J. Kim, A. Rudella, V. R. Rodriguez, Y. Asakura, Q. Sun, and K. J. van Wijk
Large Scale Comparative Proteomics of a Chloroplast Clp Protease Mutant Reveals Folding Stress, Altered Protein Homeostasis, and Feedback Regulation of Metabolism
Mol. Cell. Proteomics,
August 1, 2009;
8(8):
1789 - 1810.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
J. Kim, A. Rudella, V. Ramirez Rodriguez, B. Zybailov, P. D. B. Olinares, and K. J. van Wijk
Subunits of the Plastid ClpPR Protease Complex Have Differential Contributions to Embryogenesis, Plastid Biogenesis, and Plant Development in Arabidopsis
PLANT CELL,
June 1, 2009;
21(6):
1669 - 1692.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
R. Patel, S.-C. Hsu, J. Bedard, K. Inoue, and P. Jarvis
The Omp85-Related Chloroplast Outer Envelope Protein OEP80 Is Essential for Viability in Arabidopsis
Plant Physiology,
September 1, 2008;
148(1):
235 - 245.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
F. Yu, X. Liu, M. Alsheikh, S. Park, and S. Rodermel
Mutations in SUPPRESSOR OF VARIEGATION1, a Factor Required for Normal Chloroplast Translation, Suppress var2-Mediated Leaf Variegation in Arabidopsis
PLANT CELL,
July 1, 2008;
20(7):
1786 - 1804.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
U. Flores-Perez, S. Sauret-Gueto, E. Gas, P. Jarvis, and M. Rodriguez-Concepcion
A Mutant Impaired in the Production of Plastome-Encoded Proteins Uncovers a Mechanism for the Homeostasis of Isoprenoid Biosynthetic Enzymes in Arabidopsis Plastids
PLANT CELL,
May 1, 2008;
20(5):
1303 - 1315.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
E. Miura, Y. Kato, R. Matsushima, V. Albrecht, S. Laalami, and W. Sakamoto
The Balance between Protein Synthesis and Degradation in Chloroplasts Determines Leaf Variegation in Arabidopsis yellow variegated Mutants
PLANT CELL,
April 1, 2007;
19(4):
1313 - 1328.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
L. L.E. Sjogren, T. M. Stanne, B. Zheng, S. Sutinen, and A. K. Clarke
Structural and Functional Insights into the Chloroplast ATP-Dependent Clp Protease in Arabidopsis
PLANT CELL,
October 1, 2006;
18(10):
2635 - 2649.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
A. Rudella, G. Friso, J. M. Alonso, J. R. Ecker, and K. J. van Wijk
Downregulation of ClpR2 Leads to Reduced Accumulation of the ClpPRS Protease Complex and Defects in Chloroplast Biogenesis in Arabidopsis
PLANT CELL,
July 1, 2006;
18(7):
1704 - 1721.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
F. I. Andersson, R. Blakytny, J. Kirstein, K. Turgay, B. Bukau, A. Mogk, and A. K. Clarke
Cyanobacterial ClpC/HSP100 Protein Displays Intrinsic Chaperone Activity
J. Biol. Chem.,
March 3, 2006;
281(9):
5468 - 5475.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
J. Bedard and P. Jarvis
Recognition and envelope translocation of chloroplast preproteins
J. Exp. Bot.,
September 1, 2005;
56(419):
2287 - 2320.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
