Heterologous Expression of a Plant Small Heat-Shock Protein Enhances Escherichia Coli Viability under Heat And Cold Stress Ref.: 1

Soto de Viana, Álvaro and Allona Alberich, Isabel Marta and Collada Collada, Maria Carmen and Guevara Morato, Ángeles and Casado García, Rosa and Rodriguez Cerezo, Emilio and Aragoncillo Ballesteros, Cipriano and Gómez, Luis (1999). Heterologous Expression of a Plant Small Heat-Shock Protein Enhances Escherichia Coli Viability under Heat And Cold Stress Ref.: 1. "Plant Physiology", v. 120 ; pp. 521-528. ISSN 0032-0889.

Description

Title: Heterologous Expression of a Plant Small Heat-Shock Protein Enhances Escherichia Coli Viability under Heat And Cold Stress Ref.: 1
Author/s:
  • Soto de Viana, Álvaro
  • Allona Alberich, Isabel Marta
  • Collada Collada, Maria Carmen
  • Guevara Morato, Ángeles
  • Casado García, Rosa
  • Rodriguez Cerezo, Emilio
  • Aragoncillo Ballesteros, Cipriano
  • Gómez, Luis
Item Type: Article
Título de Revista/Publicación: Plant Physiology
Date: 1999
ISSN: 0032-0889
Volume: 120
Subjects:
Faculty: E.T.S.I. Montes (UPM)
Department: Biotecnologia [hasta 2014]
Creative Commons Licenses: Recognition - No derivative works - Non commercial

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Abstract

A small heat-shock protein (sHSP) that shows molecular chaperone activity in vitro was recently purified from mature chestnut (Castanea sativa) cotyledons. This protein, renamed here as CsHSP17.5, belongs to cytosolic class I, as revealed by cDNA sequencing and immunoelectron microscopy. Recombinant CsHSP17.5 was overexpressed in Escherichia coli to study its possible function under stress conditions. Upon transfer from 37°C to 50°C, a temperature known to cause cell autolysis, those cells that accumulated CsHSP17.5 showed improved viability compared with control cultures. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis of cell lysates suggested that such a protective effect in vivo is due to the ability of recombinant sHSP to maintain soluble cytosolic proteins in their native conformation, with little substrate specificity. To test the recent hypothesis that sHSPs may be involved in protection against cold stress, we also studied the viability of recombinant cells at 4°C. Unlike the major heat-induced chaperone, GroEL/ES, the chestnut sHSP significantly enhanced cell survivability at this temperature. CsHSP17.5 thus represents an example of a HSP capable of protecting cells against both thermal extremes. Consistent with these findings, high-level induction of homologous transcripts was observed in vegetative tissues of chestnut plantlets exposed to either type of thermal stress but not salt stress

More information

Item ID: 13923
DC Identifier: http://oa.upm.es/13923/
OAI Identifier: oai:oa.upm.es:13923
Official URL: http://www.plantphysiol.org/
Deposited by: Memoria Investigacion
Deposited on: 20 Dec 2012 11:17
Last Modified: 13 May 2015 13:01
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