3 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)6220-6227
Number of pages8
JournalApplied and Environmental Microbiology
Volume79
Issue number20
DOIs
StatePublished - 2013

Fingerprint

Synechocystis
heat shock
Heat-Shock Proteins
heat shock proteins
cell viability
heat stress
Shock
Cell Survival
Hot Temperature
tolerance
Heat-Shock Response
Thylakoids
protein
immunocytochemistry
Cyanobacteria
protein aggregates
Chlorophyll
thylakoids
Heating
cell death

ASJC Scopus subject areas

  • Applied Microbiology and Biotechnology
  • Food Science
  • Biotechnology
  • Ecology

Cite this

ClpB1 overproduction in Synechocystis sp. strain PCC 6803 increases tolerance to rapid heat shock. / Gonzalez-Esquer, C. Raul; Vermaas, Willem.

In: Applied and Environmental Microbiology, Vol. 79, No. 20, 2013, p. 6220-6227.

Research output: Contribution to journalArticle

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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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