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(Received for publication, March 17, 1997, and in revised form, May 14, 1997)
From the Department of Cell and Molecular Biology, Northwestern
University Medical School, Chicago, Illinois 60611
Nuclear respiratory factor 1 (NRF-1) is a
transcriptional activator that acts on a diverse set of nuclear genes
required for mitochondrial respiratory function in mammalian cells.
These genes encode respiratory proteins as well as components of the
mitochondrial transcription, replication, and heme biosynthetic
machinery. Here, we establish that NRF-1 is a phosphoprotein in
vivo. Phosphorylation occurs on serine residues within a concise
NH2-terminal domain with the major sites of phosphate
incorporation at serines 39, 44, 46, 47, and 52. The in
vivo phosphorylation pattern can be approximated in
vitro by phosphorylating recombinant NRF-1 with purified casein
kinase II. Phosphate incorporation at the sites utilized in
vivo results in a marked stimulation of DNA binding activity
which is not observed in mutated proteins lacking these sites. Pairwise
expression of the wild-type protein with each of a series of truncated
derivatives in transfected cells results in the formation of a dimer
between wild-type and mutant forms demonstrating that a homodimer is
the active binding species. Although NRF-1 can dimerize in the absence
of DNA, phosphorylation does not enhance the formation of these dimers.
These findings suggest that phosphorylation results in an intrinsic
change in the NRF-1 dimer enhancing its ability to bind DNA.
Volume 272, Number 30,
Issue of July 25, 1997
pp. 18732-18739
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
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