ArticleApplied and environmental microbiology2013
ClpB1 overproduction in Synechocystis sp. strain PCC 6803 increases tolerance to rapid heat shock.
Article in Applied and environmental microbiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Cyanobacteria-derived near-infrared autofluorescent exosomes enabling synergistic brain lesion imaging and neuroprotection.Bioactive materials · 2026Article
- Compensatory respiration supports survival during extended heat stress inScience advances · 2026Article
- Very high CONAR genomics and bioinformatics · 2026Article
- Application of Cyanobacteria as Chassis Cells in Synthetic Biology.Microorganisms · 2024Review
- Escherichia coli AraJ boosts utilization of arabinose in metabolically engineered cyanobacterium Synechocystis sp. PCC 6803.AMB Express · 2021Article
- State-of-the-Art Genetic Modalities to Engineer Cyanobacteria for Sustainable Biosynthesis of Biofuel and Fine-Chemicals to Meet Bio-Economy Challenges.Life (Basel, Switzerland) · 2019Review
- Highlights from the Indo-US workshop "Cyanobacteria: molecular networks to biofuels" held at Lonavala, India during December 16-20, 2012.Photosynthesis research · 2013Article
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Abstract
ClpB1 is a heat shock protein known to disaggregate large protein complexes. Constitutive, 16-fold ClpB1 overproduction in the cyanobacterium Synechocystis sp. strain PCC 6803 increased cell survival by 20-fold when cultures were heated quickly (1°C/s) to 50°C and delayed cell death by an average of 3 min during incubation at high temperatures (>46°C). Cooverexpression of ClpB1 and another heat shock protein, DnaK2, further increased cell survival. According to immunocytochemistry results, ClpB1 is dispersed throughout the cytoplasm but is concentrated in specific areas and is more prevalent near thylakoid membranes. However, ClpB1 overproduction does not lead to a change in the morphology, chlorophyll content, or photosystem ratio. Whereas electron microscopy demonstrated that apparent protein aggregation occurred after heat treatment in the control strain, protein aggregate size was maintained in the ClpB1 overexpresser. Constitutive ClpB1 overproduction allows an earlier response to heat shock and protects from rapid heating of cultures.
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