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Vol. 273, Issue 1, 349-355, January 2, 1998
From the rECH1, a recently identified rat cDNA
(FitzPatrick, D. R., Germain-Lee, E., and Valle, D. (1995)
Genomics 27, 457-466) encodes a polypeptide belonging to
the hydratase/isomerase superfamily. We modeled the structure of rECH1
based on rat mitochondrial 2-enoyl-CoA hydratase 1. The model predicts
that rECH1p has the hydratase fold in the core domain and two domains
for interaction with other subunits. When we incubated
3,5,8,11,14-eicosapentaenoyl-CoA with purified rECH1p, the spectral
data suggested a switching of the double bonds from the
3,5-2,4-Dienoyl-CoA Isomerase from
Rat Liver
MOLECULAR CHARACTERIZATION
,§,,,
,
Biocenter Oulu and Department of
Biochemistry, University of Oulu, Linnanmaa, FIN-90570 Oulu, Finland,
§ Department of Pathology, University of Oulu, Kajaaninitie
52 A, FIN-90220 Oulu, Finland, ¶ Human Genetics Unit, Molecular
Medicine Centre, University of Edinburgh EH4 2XU, United Kingdom,
Department of Biosciences, Division of Biochemistry, P. O. Box
56, FIN-00014 University of Helsinki, Finland, and ** Howard Hughes
Medical Institute, Johns Hopkins University School of Medicine,
Baltimore, Maryland 21205
3-5 to the
2-4 positions. This was confirmed by
demonstrating that the product was a valid substrate for
2,4-dienoyl-CoA reductase. These results indicate that rECH1p is
3,5-2,4-dienoyl-CoA isomerase.
Subcellular fractionation and immunoelectron microscopy using
antibodies to a synthetic polypeptide derived from the C terminus of
rECH1p showed that rECH1p is located in the matrix of both mitochondria
and peroxisomes in rat liver. Consistent with these observations, the
36,000-Da rECH1p has a potential N-terminal mitochondrial targeting
signal as well as a C-terminal peroxisomal targeting signal type 1. Transport of the protein into the mitochondria with cleavage of the
targeting signal results in a mature mitochondrial form with a
molecular mass of 32,000 Da; transport to peroxisomes yields a protein
of 36,000 Da.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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