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<title lang=en>Proteomic profiling of thermal acclimation in Drosophila melanogaster</title>
<creator>Colinet, Hervé</creator>
<creator>Overgaard, Johannes</creator>
<creator>Com, Emmanuelle</creator>
<creator>Sorensen, Jesper Givskov</creator>
<contributor>Ecosystèmes, biodiversité, évolution [Rennes] (ECOBIO) ; Université de Rennes 1 (UR1) - INEE - Observatoire des Sciences de l'Univers de Rennes (OSUR) - Centre National de la Recherche Scientifique (CNRS)</contributor>
<contributor>Aarhus University [Aarhus]</contributor>
<contributor>Plateforme Protéomique-Biogenouest (PPB) ; Institut de recherche, santé, environnement et travail [Rennes] (Irset) ; Université d'Angers (UA) - Université des Antilles et de la Guyane (UAG) - Université de Rennes 1 (UR1) - École des Hautes Études en Santé Publique [EHESP] (EHESP) - Institut National de la Santé et de la Recherche Médicale (INSERM) - Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique ) - Université d'Angers (UA) - Université des Antilles et de la Guyane (UAG) - Université de Rennes 1 (UR1) - École des Hautes Études en Santé Publique [EHESP] (EHESP) - Institut National de la Santé et de la Recherche Médicale (INSERM) - Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique ) - Proteomics Core Facility (Protim) ; Université de Rennes 1 (UR1) - Plateforme Génomique Santé Biogenouest® - Plateforme Génomique Santé Biogenouest®</contributor>
<contributor>Fonds Recherche Scientifique FNRS Belgium</contributor>
<description>International audience</description>
<source>ISSN: 0965-1748</source>
<source>Insect Biochemistry and Molecular Biology</source>
<publisher>Elsevier</publisher>
<identifier>hal-00826939</identifier>
<identifier>https://hal.archives-ouvertes.fr/hal-00826939</identifier>
<source>https://hal.archives-ouvertes.fr/hal-00826939</source>
<source>Insect Biochemistry and Molecular Biology, Elsevier, 2013, 43 (4), pp.352-365. 〈10.1016/j.ibmb.2013.01.006〉</source>
<identifier>DOI : 10.1016/j.ibmb.2013.01.006</identifier>
<relation>info:eu-repo/semantics/altIdentifier/doi/10.1016/j.ibmb.2013.01.006</relation>
<identifier>PUBMED : 23416132</identifier>
<relation>info:eu-repo/semantics/altIdentifier/pmid/23416132</relation>
<language>en</language>
<subject lang=en>Fruit fly</subject>
<subject lang=en>Cold</subject>
<subject lang=en>Thermotolerance</subject>
<subject lang=en>Proteomics</subject>
<subject lang=en>Acclimation</subject>
<subject lang=en>Heat</subject>
<subject>[SDE.BE] Environmental Sciences/Biodiversity and Ecology</subject>
<type>info:eu-repo/semantics/article</type>
<type>Journal articles</type>
<description lang=en>Thermal acclimation drastically alters thermotolerance of ectotherms, but the mechanisms determining this plastic response are not fully understood. The present study investigates the proteomic response (2D-DIGE) of adult Drosophila melanogaster acclimated at 11, 25 or 31 C. As expected 11 C-acclimation improved cold tolerance and 31 C-acclimation improved heat tolerance. We hypothesized that the marked organismal responses to acclimation could be detected at the proteomic level assuming that changes in the abundance of specific proteins are linked to the physiological changes underlying the phenotypic response. The 31 C-acclimated flies displayed a particular divergent proteomic profile where molecular chaperones made up a large number of the proteins that were modulated during heat acclimation. Many other proteins showed significant modulation during acclimation including proteins involved in iron ion and cell redox homeostasis, carbohydrate and energy metabolism, chromatin remodeling and translation, and contractile machinery. Interestingly the changes in protein abundance were often unrelated to transcriptional activity of the genes coding for the proteins, except for the most strongly expressed proteins (e.g. Hsp70). The 11 C-acclimation evoked weak proteomic response despite the marked effect on the organismal phenotype. Thus the acquired cold tolerance observed here may involve regulatory process such as posttranslational regulation rather than de novo protein synthesis.</description>
<date>2013</date>
</dc>
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