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Developmental Regulations of Heat-Shock Protein Synthesis in Unstressed and Stressed Cells

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Progress in Molecular and Subcellular Biology

Part of the book series: Progress in Molecular and Subcellular Biology ((PMSB,volume 12))

Abstract

In most cells from all organisms, heat shock and several other stress promote the synthesis of proteins which have been conserved throughout evolution, the so-called heat-shock proteins (HSPs). In Escherichia coli a dozen HSPs have been characterized and their corresponding genes cloned and sequenced; their increased expression in response to heat shock is regulated by the accumulation of the htpR gene product (Neidhardt and Van Bogelen 1987). Under normal growth conditions the cells already express significant levels of HSPs, which are for the most part coded by essential genes. Each of the following major bacterial heat-shock genes (DnaK, GroE, HtpG) has been found to have eukaryotic multigenic homologs. The 80/90 kDa eukaryotic proteins are homologs to the bacterial htpG; the 70/80 kDa proteins are related to the bacterial dnaK; the 50/60 kDa proteins are related to the bacterial groEL. However, some eukaryotic HSPs such as ubiquitin do not appear to have a bacterial counterpart. For eukaryotes, there are confusing problems of nomenclature; HSP should designate heat-inducible proteins and HSC refer to “cognate” constitutive proteins; but the distinction between HSPs and HSCs is often a matter of semantics, constitutive or stress-inducible expression can depend either on the cell type or on different genes coding for the same protein. The letters hsp or hsc are followed by the approximate molecular weight in kDa.

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  1. Biologie Moléculaire du Stress, Ecole Normale Supérieure, 46 rue d’Ulm, 75230, Paris Cedex 05, France

    M. Morange

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  1. O. Bensaude
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  2. V. Mezger
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  3. M. Morange
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  1. UA CNRS 1191 Laboratoire de Biologie Moléculaire, Université des Sciences et Technique du Languedoc, 34060, Montpellier Cedex, France

    Philippe Jeanteur

  2. National Cancer Center, Research Institute, Tsukiji 5-chome, Chuo-ku, Tokyo 104, Japan

    Yoshiyuki Kuchino

  3. Abt. Angewandte Molekularbiologie, Physiologisch-Chemisches Institut, Duesbergweg 6, 6500, Mainz, Germany

    Werner E. G. Müller

  4. Department of Biological Sciences, St. John’s University Grand Central & Utopia Parkways, Jamaica, New York, 11439, USA

    Philip L. Paine

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Bensaude, O., Mezger, V., Morange, M. (1991). Developmental Regulations of Heat-Shock Protein Synthesis in Unstressed and Stressed Cells. In: Jeanteur, P., Kuchino, Y., Müller, W.E.G., Paine, P.L. (eds) Progress in Molecular and Subcellular Biology. Progress in Molecular and Subcellular Biology, vol 12. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-76553-7_4

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