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Inactivation of the clpP1 gene for the proteolytic subunit of the ATP-dependent Clp protease in the cyanobacterium Synechococcus limits growth and light acclimation

Clarke, A K; Schelin, J LU and Porankiewicz, J (1998) In Plant Molecular Biology 37(5). p.791-801
Abstract

ClpP functions as the proteolytic subunit of the ATP-dependent Clp protease in eubacteria, mammals and plant chloroplasts. We have cloned a clpP gene, designated clpP1, from the cyanobacterium Synechococcus sp. PCC 7942. The monocistronic 591 bp gene codes for a protein 80% similar to one of four putative ClpP proteins in another cyanobacterium, Synechocystis sp. PCC 6803. The constitutive ClpP1 content in Synechococcus cultures was not inducible by high temperatures, but it did rise fivefold with increasing growth light from 50 to 175 micromol photons m(-2) s(-1). A clpP1 inactivation strain (delta clpP1) exhibited slower growth rates, especially at the higher irradiances, and changes in the proportion of the photosynthetic pigments,... (More)

ClpP functions as the proteolytic subunit of the ATP-dependent Clp protease in eubacteria, mammals and plant chloroplasts. We have cloned a clpP gene, designated clpP1, from the cyanobacterium Synechococcus sp. PCC 7942. The monocistronic 591 bp gene codes for a protein 80% similar to one of four putative ClpP proteins in another cyanobacterium, Synechocystis sp. PCC 6803. The constitutive ClpP1 content in Synechococcus cultures was not inducible by high temperatures, but it did rise fivefold with increasing growth light from 50 to 175 micromol photons m(-2) s(-1). A clpP1 inactivation strain (delta clpP1) exhibited slower growth rates, especially at the higher irradiances, and changes in the proportion of the photosynthetic pigments, chlorophyll a and phycocyanin. Many mutant cells (ca. 35%) were also severely elongated, up to 20 times longer than the wild type. The stress phenotype of delta clpP1 when grown at high light was confirmed by the induction of known stress proteins, such as the heat shock protein GroEL and the alternate form of PSII reaction center D1 protein, D1 form 2. ClpP1 content also rose significantly during short-term photoinhibition, but its loss in delta clpP1 did not exacerbate the extent of inactivation of photosynthesis, nor affect the inducible D1 exchange mechanism, indicating ClpP1 is not directly involved in D1 protein turnover.

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author
publishing date
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Contribution to journal
publication status
published
keywords
Acclimatization, Adenosine Triphosphatases, Amino Acid Sequence, Chlorophyll/analysis, Cloning, Molecular, Cyanobacteria/enzymology, Endopeptidase Clp, Enzyme Induction/radiation effects, Genes, Bacterial/genetics, Hot Temperature, Light, Light-Harvesting Protein Complexes, Molecular Sequence Data, Photosynthetic Reaction Center Complex Proteins/analysis, Photosystem II Protein Complex, Phycocyanin/analysis, Sequence Analysis, DNA, Sequence Homology, Amino Acid, Serine Endopeptidases/biosynthesis
in
Plant Molecular Biology
volume
37
issue
5
pages
11 pages
publisher
Kluwer
external identifiers
  • scopus:0032125857
ISSN
0167-4412
DOI
10.1023/A:1006016302074
language
English
LU publication?
no
id
4e0db7c3-7705-4b03-955b-abaa3fd62a48
date added to LUP
2018-06-11 11:50:59
date last changed
2018-11-21 21:40:16
@article{4e0db7c3-7705-4b03-955b-abaa3fd62a48,
  abstract     = {<p>ClpP functions as the proteolytic subunit of the ATP-dependent Clp protease in eubacteria, mammals and plant chloroplasts. We have cloned a clpP gene, designated clpP1, from the cyanobacterium Synechococcus sp. PCC 7942. The monocistronic 591 bp gene codes for a protein 80% similar to one of four putative ClpP proteins in another cyanobacterium, Synechocystis sp. PCC 6803. The constitutive ClpP1 content in Synechococcus cultures was not inducible by high temperatures, but it did rise fivefold with increasing growth light from 50 to 175 micromol photons m(-2) s(-1). A clpP1 inactivation strain (delta clpP1) exhibited slower growth rates, especially at the higher irradiances, and changes in the proportion of the photosynthetic pigments, chlorophyll a and phycocyanin. Many mutant cells (ca. 35%) were also severely elongated, up to 20 times longer than the wild type. The stress phenotype of delta clpP1 when grown at high light was confirmed by the induction of known stress proteins, such as the heat shock protein GroEL and the alternate form of PSII reaction center D1 protein, D1 form 2. ClpP1 content also rose significantly during short-term photoinhibition, but its loss in delta clpP1 did not exacerbate the extent of inactivation of photosynthesis, nor affect the inducible D1 exchange mechanism, indicating ClpP1 is not directly involved in D1 protein turnover.</p>},
  author       = {Clarke, A K and Schelin, J and Porankiewicz, J},
  issn         = {0167-4412},
  keyword      = {Acclimatization,Adenosine Triphosphatases,Amino Acid Sequence,Chlorophyll/analysis,Cloning, Molecular,Cyanobacteria/enzymology,Endopeptidase Clp,Enzyme Induction/radiation effects,Genes, Bacterial/genetics,Hot Temperature,Light,Light-Harvesting Protein Complexes,Molecular Sequence Data,Photosynthetic Reaction Center Complex Proteins/analysis,Photosystem II Protein Complex,Phycocyanin/analysis,Sequence Analysis, DNA,Sequence Homology, Amino Acid,Serine Endopeptidases/biosynthesis},
  language     = {eng},
  number       = {5},
  pages        = {791--801},
  publisher    = {Kluwer},
  series       = {Plant Molecular Biology},
  title        = {Inactivation of the clpP1 gene for the proteolytic subunit of the ATP-dependent Clp protease in the cyanobacterium Synechococcus limits growth and light acclimation},
  url          = {http://dx.doi.org/10.1023/A:1006016302074},
  volume       = {37},
  year         = {1998},
}