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In order to characterize Sterling's triiodothyronine
(T
Volume 270,
Number 27,
Issue of July 07, pp. 16347-16354, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
1 Is Located in the Mitochondrial Matrix of Rat
Liver
) mitochondrial receptor using photoaffinity labeling, we
observed two specific T-binding proteins in the inner
membrane (28 kDa) and in the matrix (43 kDa) of rat liver mitochondria.
Western blots and immunoprecipitation using antibodies raised against
the T-binding domain of the T nuclear receptor
c-Erb A 
1 indicated that at least the 43-kDa protein was c-Erb A
1-related. In addition, gel mobility shift assays demonstrated the
occurrence of a c-Erb A 1-related mitochondrial protein that
specifically binds to a natural or a palindromic thyroid-responsive
element. Moreover, this protein specifically binds to a direct repeat 2
sequence located in the D-loop of the mitochondrial genome.
Furthermore, electron microscopy studies allowed the direct observation
of a c-Erb A-related protein in mitochondria. Lastly, the relative
amounts of the 43-kDa protein related to c-Erb A 1 were in good
correlation with the known mitochondrial mass in three typical tissues.
Interestingly, expression of a truncated form of the c-Erb A 1
nuclear receptor in CV1 cells was associated with a mitochondrial
localization and a stimulation of mitochondrial activity. These results
supply evidence of the localization of a member of the nuclear receptor
superfamily in the mitochondrial matrix involved in the regulation of
mitochondrial activity that could act as a mitochondrial
T-dependent transcription factor.
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