Functional analysis of skunk cabbage SfUCPB, a unique uncoupling protein lacking the fifth transmembrane domain, in yeast cells

Skunk cabbage, Symplocarpus foetidus, expresses two uncoupling proteins (UCPs), termed SfUCPA and SfUCPB, in the thermogenic organ spadix. SfUCPB exhibits unique structural features characterized by the absence of the putative fifth transmembrane domain (TM5) observed in SfUCPA, which is structurall...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2006-10, Vol.349 (1), p.383-390
Main Authors: Ito, Kikukatsu, Matsukawa, Kazushige, Kato, Yoshiaki
Format: Article
Language:English
Subjects:
Adenosine Triphosphate - metabolism
Amino Acid Sequence
Animals
Brassica
Genetic Vectors
Ion Channels - chemistry
Ion Channels - physiology
Membrane Potentials
Mitochondria - metabolism
Mitochondrial membrane potential
Mitochondrial Proteins - chemistry
Mitochondrial Proteins - physiology
Molecular Sequence Data
Oxygen Consumption
Plant Proteins - chemistry
Protein Structure, Tertiary
Sequence Homology, Amino Acid
SfUCPB
Skunk cabbage
Symplocarpus foetidus
Uncoupling protein
Uncoupling Protein 1
Yeast
Yeasts - metabolism
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Summary:Skunk cabbage, Symplocarpus foetidus, expresses two uncoupling proteins (UCPs), termed SfUCPA and SfUCPB, in the thermogenic organ spadix. SfUCPB exhibits unique structural features characterized by the absence of the putative fifth transmembrane domain (TM5) observed in SfUCPA, which is structurally similar to UCP1, and is abundantly expressed in the thermogenic spadix. Here, we conducted a series of comparative analyses of UCPs with six transmembrane domains, SfUCPA and rat UCP1, and TM5-deficient SfUCPB, using a heterologous yeast expression system. All UCPs were successfully expressed and targeted to the mitochondria, although the expression level of SfUCPB protein was approximately 10% of rat UCP1. The growth rate, mitochondrial membrane potential, and ATP content were significantly lower in cells expressing SfUCPB than in those expressing rat UCP1 and SfUCPA. These results suggest that SfUCPB, a novel TM5-deficient UCP, acts as an uncoupling protein in yeast cells.
ISSN:0006-291X
1090-2104
DOI:10.1016/j.bbrc.2006.08.058