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Journal of Experimental Biology, Vol 203, Issue 6 1017-1025, Copyright © 2000 by Company of Biologists
JOURNAL ARTICLES |
OG Zatsepina, KA Ulmasov, SF Beresten, VB Molodtsov, SA Rybtsov and MB Evgen'ev
Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow 117984, Russia.
We compare the properties and activation of heat-shock transcription factor (HSF1) and the synthesis of a major family of heat-shock proteins (HSP70) in lizard species inhabiting ecological niches with strikingly different thermal parameters. Under normal non-heat-shock conditions, all desert-dwelling lizard species studied so far differ from a northern, non-desert species (Lacerta vivipara) in the electrophoretic mobility and content of proteins constitutively bound to the regulatory heat-shock elements in the heat-shock gene promoter. Under these conditions, levels of activated HSF1 and of both HSP70 mRNA and protein are higher in the desert species than in the non-desert species. Upon heat shock, HSF1 aggregates in all species studied, although in desert species HSF1 subsequently disaggregates more rapidly. Cells of the northern species have a lower thermal threshold for HSP expression than those of the desert species, which correlates with the relatively low constitutive level of HSPs and high basal content of HSF1 in their cells.
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