The Function of Heat-Shock Proteins in Stress Tolerance: Degradation and Reactivation of Damaged Proteins

The Function of Heat-Shock Proteins in Stress Tolerance: Degradation and Reactivation of Damaged... Organisms respond to sudden increases in temperature by synthesizing a small set of proteins called the heat-shock proteins (hsps) (See Figure 1 ) . This heat-shock response has been highly conserved throughout evolution, not only as a physiological phenomenon, but also at the level of the individual proteins . Hsps comprise some of the most highly conserved protein families known. The level of amino-acid identity between all prokaryotic and eukaryotic hsp70 proteins, for example, approaches 50% (95). Hsp families often include constitutive as well as heat-inducible C �c:P HS C Q'� HS -hspl00 - hIp9O - -� hsp70 Figure 1 Induction o f heat-shock proteins. Logarithmically growing cells were pulse-labeled 3 with H-leucine either while growing at nonnal temperatures (E. coli, 37°C; S. cerevisiae, 25°C; D. melanogaster, 25°C) or following a shift to slightly elevated temperatures (E. coli, 50°C, 10 min; S. cerevisiae, 39°C, 20 min; D. melanogaster, 36.5°C, 45 min). Total cellular proteins were from (15Ia). extracted, separated on a 10% SDS-polyacrylamide gel, and visualized by fluorography. Figure Table 1 Protein family hsplOO Major heat-shock protein families Monomer Family members hsp104, ClpA, ClpB, ClpC, ClpX 46 kd (ClpX) size (kd) 80-ll0 kd Eukaryotic location Cytoplasm, nucleus, nucleolus, http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Annual Review of Genetics Annual Reviews

The Function of Heat-Shock Proteins in Stress Tolerance: Degradation and Reactivation of Damaged Proteins

Annual Review of Genetics, Volume 27 (1) – Dec 1, 1993

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Publisher
Annual Reviews
Copyright
Copyright 1993 Annual Reviews. All rights reserved
Subject
Review Articles
ISSN
0066-4197
eISSN
1545-2948
D.O.I.
10.1146/annurev.ge.27.120193.002253
Publisher site
See Article on Publisher Site

Abstract

Organisms respond to sudden increases in temperature by synthesizing a small set of proteins called the heat-shock proteins (hsps) (See Figure 1 ) . This heat-shock response has been highly conserved throughout evolution, not only as a physiological phenomenon, but also at the level of the individual proteins . Hsps comprise some of the most highly conserved protein families known. The level of amino-acid identity between all prokaryotic and eukaryotic hsp70 proteins, for example, approaches 50% (95). Hsp families often include constitutive as well as heat-inducible C �c:P HS C Q'� HS -hspl00 - hIp9O - -� hsp70 Figure 1 Induction o f heat-shock proteins. Logarithmically growing cells were pulse-labeled 3 with H-leucine either while growing at nonnal temperatures (E. coli, 37°C; S. cerevisiae, 25°C; D. melanogaster, 25°C) or following a shift to slightly elevated temperatures (E. coli, 50°C, 10 min; S. cerevisiae, 39°C, 20 min; D. melanogaster, 36.5°C, 45 min). Total cellular proteins were from (15Ia). extracted, separated on a 10% SDS-polyacrylamide gel, and visualized by fluorography. Figure Table 1 Protein family hsplOO Major heat-shock protein families Monomer Family members hsp104, ClpA, ClpB, ClpC, ClpX 46 kd (ClpX) size (kd) 80-ll0 kd Eukaryotic location Cytoplasm, nucleus, nucleolus,

Journal

Annual Review of GeneticsAnnual Reviews

Published: Dec 1, 1993

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