First published online April 18, 2008
Journal of Experimental Biology 211, 1456-1462 (2008)
Published by The Company of Biologists 2008
doi: 10.1242/jeb.012328
Reptilian uncoupling protein: functionality and expression in sub-zero temperatures
Benjamin Rey1,
Brigitte Sibille1,
Caroline Romestaing1,
Maud Belouze1,
Dominique Letexier1,
Stéphane Servais1,
Hervé Barré1,
Claude Duchamp1 and
Yann Voituron2,*
1 Laboratoire de Physiologie Intégrative, cellulaire et
moléculaire, Centre National de la Recherche Scientifique (CNRS)
– Université Claude Bernard Lyon 1, 43 Bvd 11 Novembre 1918,
F-69622 Villeurbanne Cedex, France
2 Station d'Ecologie Expérimentale du CNRS à Moulis, Laboratoire
Evolution et Diversité du Vivant, Moulis, F-09200 Saint-Girons,
France

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Fig. 1. Partial predicted amino acid sequence and alignment of repUCP with other
homologues of mammalian UCPs. The asterisks indicate amino acid preserved in
all presented UCPs. A black background indicates the nucleotides that are
essential for GDP binding (Arg83, Arg182 and
Hist214) and that they are present in all the mammalian UCP
homologues.
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Fig. 2. Tissue distribution of repUCP mRNA (390 bp) in Lacerta vivipara
after 32 cycles of PCR. Lane 1 is a 100 pb ladder, lanes 2–7 show
expression of reptilian UCP in liver, skeletal muscle, lung, heart, brain and
adipose tissue, respectively, from one representative individual.
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Fig. 4. Representative experimental traces of oxygen consumption by muscle
mitochondria from control lizard energised with succinate (for details, see
Materials and methods). (A) Mitochondrial state 4, state 3 (addition of 1 mmol
l–1 ADP) and state 4+ (addition of 1 µg
ml–1 oligomycin). (B) Effect of two sequential additions of 1
mmol l–1 GDP on state 4 mitochondrial oxygen consumption.
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© The Company of Biologists Ltd 2008