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 ï¿½c:P HS C Q'ï¿½ HS -hspl00 - hIp9O - -ï¿½ 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, 37Â°C; S. cerevisiae, 25Â°C; D. melanogaster, 25Â°C) or following a shift to slightly elevated temperatures (E. coli, 50Â°C, 10 min; S. cerevisiae, 39Â°C, 20 min; D. melanogaster, 36.5Â°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,
Annual Review of Genetics – Annual Reviews
Published: Dec 1, 1993
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