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Proteome stability, heat hardening and heat-shock protein expression profiles in Cataglyphis desert ants.
Willot, Quentin; Gueydan, Cyril; Aron, Serge.
Afiliação
  • Willot Q; Evolutionary Biology and Ecology, Université Libre de Bruxelles, 1050 Brussels, Belgium Quentin.Willot@ulb.ac.be.
  • Gueydan C; Molecular Biology of the Gene, Université Libre de Bruxelles, 6041 Charleroi (Gosselies), Belgium.
  • Aron S; Evolutionary Biology and Ecology, Université Libre de Bruxelles, 1050 Brussels, Belgium.
J Exp Biol ; 220(Pt 9): 1721-1728, 2017 05 01.
Article em En | MEDLINE | ID: mdl-28232398
ABSTRACT
In ectotherms, high temperatures impose physical limits, impeding activity. Exposure to high heat levels causes various deleterious and lethal effects, including protein misfolding and denaturation. Thermophilic ectotherms have evolved various ways to increase macromolecular stability and cope with elevated body temperatures; these include the high constitutive expression of molecular chaperones. In this study, we investigated the effect of moderate to severe heat shock (37-45°C) on survival, heat hardening, protein damage and the expression of five heat tolerance-related genes (hsc70-4 h1, hsc70-4 h2, hsp83, hsc70-5 and hsf1) in two closely related Cataglyphis ants that occur in distinct habitats. Our results show that the highly thermophilic Sahara ant Cataglyphis bombycina constitutively expresses HSC70 at higher levels, but has lower induced expression of heat tolerance-related genes in response to heat shock, as compared with the more mesophilic Cataglyphis mauritanica found in the Atlas Mountains. As a result, C. bombycina demonstrates increased protein stability when exposed to acute heat stress but is less disposed to acquiring induced thermotolerance via heat hardening. These results provide further insight into the evolutionary plasticity of the hsp gene expression system and subsequent physiological adaptations in thermophilous desert insects to adapt to harsh environmental conditions.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Formigas / Proteoma / Proteínas de Choque Térmico Idioma: En Ano de publicação: 2017 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Formigas / Proteoma / Proteínas de Choque Térmico Idioma: En Ano de publicação: 2017 Tipo de documento: Article