Heat stress management in synechocystis PCC 6803

The interplay between membranes and stress protein molecular chaperones

Research output: Chapter in Book/Report/Conference proceedingChapter

Abstract

Exposure of organisms to a sudden increase in temperature triggers a ubiquitous and homeostatic cellular stress response. This heat shock response is characterized by rapid induction of genes encoding heat shock proteins (HSPs), which are divided into seven functional classes: metabolism, DNA/RNA repair, protein degradation, regulation, transport, cell organization, and molecular chaperones [1], and references therein. An almost identical functional classification of stress proteins was suggested by Kültz [2]. The predominant class of HSPs, the molecular chaperones [3], comprises five major and evolutionarily conserved families-ClpB (in eukaryotes HSP100), HtpG (HSP90), dnaK (HSP70), GroESL also called as chaperonins (HSP60), and small heat shock proteins (sHSPs). Under physiological conditions, they assist in several important cellular processes including the correct folding of de novo synthesized proteins, the assembly of oligomeric structures, the membrane transport of proteins, etc. [4]. Upon heat stress, polypeptides tend to lose their native conformation, which leads to the increased exposure of hydrophobic amino acid sequences normally buried inside the molecule. Molecular chaperones are able to recognize these patches and help to prevent their aggregation and facilitate the refolding of the damaged proteins [1,5]. Based on their activity, chaperones can be divided into three classes. “Foldases” (dnaK, GroEL) assist in the correct (re)-folding of polypeptides together with their co-chaperones. The “holdases” (sHSPs and HtpGs) are able to bind nonnative proteins and prevent their aggregation, but do not directly facilitate their folding. The third class of chaperones (“unfoldases/disaggregases,” ClpB family) is capable to dissolve aggregates [1,5,6].

Original languageEnglish
Title of host publicationStress Biology of Cyanobacteria
Subtitle of host publicationMolecular Mechanisms to Cellular Responses
PublisherCRC Press
Pages145-154
Number of pages10
ISBN (Electronic)9781466575196
ISBN (Print)9781466504783
DOIs
Publication statusPublished - Jan 1 2013

Fingerprint

stress management
Synechocystis
molecular chaperones
Molecular Chaperones
Heat-Shock Proteins
heat shock proteins
Small Heat-Shock Proteins
heat stress
Membrane Proteins
Hot Temperature
Protein Refolding
Chaperonins
Heat-Shock Response
polypeptides
Peptides
Membrane Transport Proteins
proteins
Eukaryota
chaperonins
DNA Repair

ASJC Scopus subject areas

  • Agricultural and Biological Sciences(all)
  • Immunology and Microbiology(all)

Cite this

Heat stress management in synechocystis PCC 6803 : The interplay between membranes and stress protein molecular chaperones. / Glatz, A.; Török, Z.; Vígh, L.; Horváth, I.

Stress Biology of Cyanobacteria: Molecular Mechanisms to Cellular Responses. CRC Press, 2013. p. 145-154.

Research output: Chapter in Book/Report/Conference proceedingChapter

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