Sökning: WFRF:(Clarke S. M.)
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Structural and func...
Structural and functional insights into the chloroplast ATP-dependent Clp protease in Arabidopsis
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- Sjögren, Lars, 1977 (författare)
- Gothenburg University,Göteborgs universitet,Institutionen för växt- och miljövetenskaper,Department of Plant and Environmental Sciences
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- Stanne, Tara M, 1979 (författare)
- Gothenburg University,Göteborgs universitet,Institutionen för växt- och miljövetenskaper,Department of Plant and Environmental Sciences
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- Zheng, Bo (författare)
- Umeå universitet,Institutionen för fysiologisk botanik,Umeå Plant Science Centre (UPSC)
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Sutinen, S. (författare)
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- Clarke, Adrian K, 1964 (författare)
- Gothenburg University,Göteborgs universitet,Institutionen för växt- och miljövetenskaper,Department of Plant and Environmental Sciences
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(creator_code:org_t)
- 2006-09-15
- 2006
- Engelska.
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Ingår i: Plant Cell. - : Oxford University Press (OUP). - 1040-4651 .- 1532-298X. ; 18:10, s. 2635-2649
- Relaterad länk:
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http://www.plantcell...
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https://gup.ub.gu.se...
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https://doi.org/10.1...
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https://urn.kb.se/re...
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Abstract
Ämnesord
Stäng
- 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.
Ämnesord
- NATURVETENSKAP -- Biologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences (hsv//eng)
Nyckelord
- PLANT DEVELOPMENT
- NORWAY SPRUCE
- COMPLEX
- IDENTIFICATION
- GENE
- THALIANA
- PROTEINS
- FTSH
- BIOSYNTHESIS
- DEGRADATION
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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