ArticlePlant molecular biology1996
The cyanobacterium Synechococcus sp. PCC 7942 possesses a close homologue to the chloroplast ClpC protein of higher plants.
Article in Plant molecular biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed, 42 citations in OpenAlex.
- Cloning of some heat shock proteins genes for further transcriptional study of Planktothrix agardhii exposed to abiotic stress.Folia microbiologica · 2015Article
- The quantitative proteomic response of Synechocystis sp. PCC6803 to phosphate acclimation.Aquatic biosystems · 2013Article
- Article
- The apicomplexan plastid and its evolution.Cellular and molecular life sciences : CMLS · 2011Review
- Structure and function of a novel type of ATP-dependent Clp protease.The Journal of biological chemistry · 2009Article
- Complexity of rice Hsp100 gene family: lessons from rice genome sequence data.Journal of biosciences · 2007Article
- 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.Plant physiology · 2004Article
- A stromal Hsp100 protein is required for normal chloroplast development and function in Arabidopsis.Plant physiology · 2004Article
- Novel form of ClpB/HSP100 protein in the cyanobacterium Synechococcus.Journal of bacteriology · 2001Article
- Chloroplast-targeted ERD1 protein declines but its mRNA increases during senescence in Arabidopsis.Plant physiology · 1999Article
- Inactivation of the clpP1 gene for the proteolytic subunit of the ATP-dependent Clp protease in the cyanobacterium Synechococcus limits growth and light acclimation.Plant molecular biology · 1998Article
- Induction of the heat shock protein ClpB affects cold acclimation in the cyanobacterium Synechococcus sp. strain PCC 7942.Journal of bacteriology · 1997Article
- Protein stability and degradation in chloroplasts.Plant molecular biology · 1996Review
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2 authors at 1 institution in 1 country.
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Abstract
The Clp family consists of large, ubiquitous proteins that function as molecular chaperones and/or regulators of ATP-dependent proteolysis. A single copy gene coding for one of these proteins, ClpC, was cloned from the unicellular cyanobacterium Synechococcus sp. PCC 7942. The predicted polypeptide is most similar (ca. 88%) to the chloroplast-localized ClpC protein from higher plants. Using degenerate PCR primers specific for the two distinct ATP-binding domains characteristic of all ClpA-C proteins, partial sequences homologous to clpC from Synechococcus were also identified in five other cyanobacterial strains. The Synechococcus clpC gene is transcribed under standard growth conditions as a monocistronic message of around 2.7 kb. The level of this message, however, decreases slightly after a shift from 37 to 47.5 degrees C for 2 h, similar to expression previously observed for clpC mRNA from heat-shocked higher plants. At the protein level, the amount of ClpC remains relatively unchanged during the high temperature shift, while that of the known heat shock protein GroEL rises considerably. In contrast, the constitutive level of ClpC in Synechococcus increases considerably under conditions of rapid growth, both with increasing light intensities or CO2 concentrations. This, and the fact that attempts to inactivate clpC expression fail to produce a viable phenotype, suggest that ClpC activity is essential for growth in this obligate photoautotrophic cyanobacterium.
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