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Titlebook: Heat Shock; Bruno Maresca,Susan Lindquist Conference proceedings 1991 Springer-Verlag Berlin Heidelberg 1991 Gene Regulation.Genregulierun

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Mechanisms of Regulation of Small Heat Shock Protein Genes in ,evealed that the two stimuli regulate gene expression by distinct mechanisms. Sequence elements that are critically important for ecdysterone activation of the . and . genes have been identified and have been used to purify ecdysterone receptor by specific DNA affinity chromatography. Purified recep
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DnaJ and DnaK Heat Shock Proteins Activate Sequence Specific DNA Binding by RepAisassembly of oligomeric protein structures (for review see Rothman, 1989). The mechanisms by which heat shock proteins (HSPs) catalyze these reactions have not been elucidated and are the object of great interest, particularly in view of their ubiquity and high conservation during evolution (for re
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Ubiquitin-Conjugating Enzymes Mediate Essential Functions of the Stress Responsettachment of ubiquitin to proteolytic substrates and their subsequent degradation by a specific ATP-dependent protease complex. We have cloned the genes and characterized the function of seven ubiquitin-conjugating enzymes (UBCs) from the yeast .. From this collection, UBC1, UBC4 and UBC5 enzymes we
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Early Effects of Heat Shock on Enzymes: Heat Denaturation of Reporter Proteins and Activation of a P on indirect arguments developped by several workers (Hightower, 1980). The fate of such denatured proteins is matter for discussion: are they degraded or renatured? A priming non-lethal heat-shock stimulates transiently the synthesis of the heat-shock proteins (HSP) and increases transiently the ce
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Inhibition of Nascent Polypeptide Formation by HSP70 Proteins wheat germ and several different mRNAs. Inhibition was dose-dependent over a range of 0.1–0.4 nmoles of HSP70 and more pronounced at low temperatures. When bromo mosaic virus mRNAs were tested, inhibition was greater for the larger polypeptides indicating that HSP70 blocks nascent polypeptide elong
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