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An Arabidopsis thal...
An Arabidopsis thaliana virescent mutant reveals a role for ClpR1 in plastid development
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Koussevitzky, S. (author)
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- Stanne, Tara M, 1979 (author)
- Gothenburg University,Göteborgs universitet,Institutionen för växt- och miljövetenskaper,Department of Plant and Environmental Sciences
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Peto, C. A. (author)
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Giap, T. (author)
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- Sjögren, Lars, 1977 (author)
- Gothenburg University,Göteborgs universitet,Institutionen för växt- och miljövetenskaper,Department of Plant and Environmental Sciences
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Zhao, Y. D. (author)
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- Clarke, Adrian K, 1964 (author)
- Gothenburg University,Göteborgs universitet,Institutionen för växt- och miljövetenskaper,Department of Plant and Environmental Sciences
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Chory, J. (author)
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(creator_code:org_t)
- 2006-09-29
- 2007
- English.
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In: Plant Molecular Biology. - : Springer Science and Business Media LLC. - 0167-4412 .- 1573-5028. ; 63:1, s. 85-96
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Abstract
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- The ATP-dependent Clp protease has been well-characterized in Escherichia coli, but knowledge of its function in higher plants is limited. In bacteria, this two-component protease consists of a Ser-type endopeptidase ClpP, which relies on the ATP-dependent unfolding activity from an Hsp100 molecular chaperone to initiate protein degradation. In the chloroplasts of higher plants, multiple isoforms of the proteolytic subunit exist, with Arabidopsis having five ClpPs and four ClpP-like proteins termed ClpR predicted in its genome. In this work we characterized an Arabidopsis mutant impaired in one subunit of the chloroplast-localized Clp protease core, ClpR1. clpR1-1, a virescent mutant, carries a pre-mature stop codon in the clpR1 gene, resulting in no detectable ClpR1 protein. The accumulation of several chloroplast proteins, as well as most of the chloroplast-localized Clp protease subunits, is inhibited in clpR1-1. Unexpectedly, some plastid-encoded proteins do not accumulate, although their transcripts accumulate to wild-type levels. Maturation of 23S and 4.5S chloroplast ribosomal RNA (cp-rRNA) is delayed in clpR1-1, and both RNAs accumulate as higher molecular weight precursors. Also, chloroplasts in clpR1-1 are smaller than in wild type and have fewer thylakoid membranes with smaller grana stacks. We propose that a ClpR1-containing activity is required for chloroplast development and differentiation and in its absence both are delayed.
Subject headings
- NATURVETENSKAP -- Biologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences (hsv//eng)
Keyword
- Arabidopsis thaliana
- virescent
- chloroplast development
- Clp protease
- ATP-DEPENDENT PROTEASE
- CHLOROPLAST DEVELOPMENT
- ESCHERICHIA-COLI
- MOLECULAR CHAPERONE
- LEAF VARIEGATION
- RIBOSOMAL-RNAS
- FTSH
- GENE
- ENCODES
- DEGRADATION
Publication and Content Type
- ref (subject category)
- art (subject category)
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- By the author/editor
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Koussevitzky, S.
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Stanne, Tara M, ...
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Peto, C. A.
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Giap, T.
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Sjögren, Lars, 1 ...
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Zhao, Y. D.
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show more...
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Clarke, Adrian K ...
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Chory, J.
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- About the subject
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- NATURAL SCIENCES
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NATURAL SCIENCES
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and Biological Scien ...
- Articles in the publication
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Plant Molecular ...
- By the university
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University of Gothenburg