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Structural and Functional Insights into the Chloroplast ATP-Dependent Clp Protease in Arabidopsis
Umeå University, Faculty of Science and Technology, Plant Physiology. Umeå Plant Science Centre.
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2006 (English)In: The Plant Cell, Vol. 18, 2635-2649 p.Article in journal (Refereed) Published
Abstract [en]

In contrast with the model Escherichia coli Clp protease, the ATP-dependent Clp protease in higher plants has a remarkably diverse proteolytic core consisting of multiple ClpP and ClpR paralogs, presumably arranged within a dual heptameric ring structure. Using antisense lines for the nucleus-encoded ClpP subunit, ClpP6, we show that the Arabidopsis thaliana Clp protease is vital for chloroplast development and function. Repression of ClpP6 produced a proportional decrease in the Clp proteolytic core, causing a chlorotic phenotype in young leaves that lessened upon maturity. Structural analysis of the proteolytic core revealed two distinct subcomplexes that likely correspond to single heptameric rings, one containing the ClpP1 and ClpR1-4 proteins, the other containing ClpP3-6. Proteomic analysis revealed several stromal proteins more abundant in clpP6 antisense lines, suggesting that some are substrates for the Clp protease. A proteolytic assay developed for intact chloroplasts identified potential substrates for the stromal Clp protease in higher plants, most of which were more abundant in young Arabidopsis leaves, consistent with the severity of the chlorotic phenotype observed in the clpP6 antisense lines. The identified substrates all function in more general housekeeping roles such as plastid protein synthesis, folding, and quality control, rather than in metabolic activities such as photosynthesis.

Place, publisher, year, edition, pages
2006. Vol. 18, 2635-2649 p.
URN: urn:nbn:se:umu:diva-15953DOI: doi:10.1105/tpc.106.044594OAI: diva2:155625
Available from: 2007-08-06 Created: 2007-08-06 Last updated: 2011-01-11Bibliographically approved

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Zheng, Bo
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Plant PhysiologyUmeå Plant Science Centre

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