Literature DB >> 10688700

HSP16.6 is involved in the development of thermotolerance and thylakoid stability in the unicellular cyanobacterium, Synechocystis sp. PCC 6803.

S Lee1, H A Owen, D J Prochaska, S R Barnum.   

Abstract

The low molecular weight (LMW) heat shock protein (HSP), HSP16.6, in the unicellular cyanobacterium, Synechocystis sp. PCC 6803, protects cells from elevated temperatures. A 95% reduction in the survival of mutant cells with an inactivated hsp16.6 was observed after exposure for 1 h at 47 degrees C. Wild-type cell survival was reduced to only 41%. HSP16.6 is also involved in the development of thermotolerance. After a sublethal heat shock at 43 degrees C for 1 h and subsequent challenge exposure at 49 degrees C for 40 min, mutant cells did not survive, while 64% of wild-type cells survived. Ultrastructural changes in the integrity of thylakoid membranes of heat-shocked mutant cells also are discussed. These results demonstrate an important protective role for HSP16.6 in the protection of cells and, in particular, thylakoid membrane against thermal stress.

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Year:  2000        PMID: 10688700     DOI: 10.1007/s002849910056

Source DB:  PubMed          Journal:  Curr Microbiol        ISSN: 0343-8651            Impact factor:   2.188


  18 in total

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Journal:  Microbiol Mol Biol Rev       Date:  2002-03       Impact factor: 11.056

2.  The Chlamydomonas genome reveals its secrets: chaperone genes and the potential roles of their gene products in the chloroplast.

Authors:  Michael Schroda
Journal:  Photosynth Res       Date:  2004       Impact factor: 3.573

3.  Heat shock proteins and resistance to desiccation in congeneric land snails.

Authors:  Tal Mizrahi; Joseph Heller; Shoshana Goldenberg; Zeev Arad
Journal:  Cell Stress Chaperones       Date:  2009-12-02       Impact factor: 3.667

Review 4.  Integrating protein homeostasis strategies in prokaryotes.

Authors:  Axel Mogk; Damon Huber; Bernd Bukau
Journal:  Cold Spring Harb Perspect Biol       Date:  2011-04-01       Impact factor: 10.005

5.  Hsp70 displaces small heat shock proteins from aggregates to initiate protein refolding.

Authors:  Szymon Żwirowski; Agnieszka Kłosowska; Igor Obuchowski; Nadinath B Nillegoda; Artur Piróg; Szymon Ziętkiewicz; Bernd Bukau; Axel Mogk; Krzysztof Liberek
Journal:  EMBO J       Date:  2017-02-20       Impact factor: 11.598

6.  Synechocystis HSP17 is an amphitropic protein that stabilizes heat-stressed membranes and binds denatured proteins for subsequent chaperone-mediated refolding.

Authors:  Z Török; P Goloubinoff; I Horváth; N M Tsvetkova; A Glatz; G Balogh; V Varvasovszki; D A Los; E Vierling; J H Crowe; L Vigh
Journal:  Proc Natl Acad Sci U S A       Date:  2001-02-27       Impact factor: 11.205

Review 7.  Cellular strategies for controlling protein aggregation.

Authors:  Jens Tyedmers; Axel Mogk; Bernd Bukau
Journal:  Nat Rev Mol Cell Biol       Date:  2010-10-14       Impact factor: 94.444

8.  A mutant small heat shock protein with increased thylakoid association provides an elevated resistance against UV-B damage in synechocystis 6803.

Authors:  Zsolt Balogi; Ottilia Cheregi; Kim C Giese; Kata Juhász; Elizabeth Vierling; Imre Vass; László Vígh; Ibolya Horváth
Journal:  J Biol Chem       Date:  2008-06-23       Impact factor: 5.157

9.  Small heat-shock proteins regulate membrane lipid polymorphism.

Authors:  Nelly M Tsvetkova; Ibolya Horváth; Zsolt Török; Willem F Wolkers; Zsolt Balogi; Natalia Shigapova; Lois M Crowe; Fern Tablin; Elizabeth Vierling; John H Crowe; László Vigh
Journal:  Proc Natl Acad Sci U S A       Date:  2002-10-04       Impact factor: 11.205

10.  The Hsp27 gene is not required for Drosophila development but its activity is associated with starvation resistance.

Authors:  Xinming Hao; Sen Zhang; Benjamin Timakov; Ping Zhang
Journal:  Cell Stress Chaperones       Date:  2007       Impact factor: 3.667

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