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J Biol Chem, Vol. 274, Issue 31, 22002-22007, July 30, 1999

Marked Instability of the ³² Heat Shock Transcription Factor at High Temperature
IMPLICATIONS FOR HEAT SHOCK REGULATION

From the HSP Research Institute, Kyoto Research Park, Kyoto 600-8813, Japan

The heat shock response in Escherichia coli depends on a transient increase in the intracellular level of ³² that results from both increased synthesis and transient stabilization of normally unstable ³². Although the membrane-bound ATP-dependent protease FtsH (HflB) plays an important role in degradation of ³², our previous results suggested that several cytosolic ATP-dependent proteases including HslVU (ClpQY) are also involved in ³² degradation (Kanemori, M., Nishihara, K., Yanagi, H., and Yura, T. (1997) J. Bacteriol. 179, 7219-7225). We now report on the ATP-dependent proteolysis of ³² by purified HslVU protease and its unusual dependence on high temperature: ³² was rapidly degraded at 44 °C, but with much slower rates (~15-fold) at 35 °C. FtsH-dependent degradation of ³² also gave similar results. In agreement with these results in vitro, the turnover of ³² in normally growing cells at high temperature (42 °C) was much faster than at low temperature (30 °C). Taken together with other evidence, these results suggest that the ³² level during normal growth is primarily determined by the stability (susceptibility to proteases) and synthesis rate of ³² set by ambient temperature, whereas fine adjustment such as transient stabilization of ³² observed upon heat shock is brought about through monitoring changes in the cellular state of protein folding.

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