Nucleic Acids Research, Vol 27, Issue 17 3518-3526, Copyright © 1999 by Oxford University Press
J Deckert, RA Khalaf, SM Hwang and RS Zitomer
The yeast Rox1 hypoxic transcriptional repressor protein binds to and bends
a specific DNA sequence through an HMG domain located at the N- terminus.
To better understand the structure of Rox1 and how it interacts with DNA,
38 missense mutations in the HMG domain were isolated through a combination
of random and site-directed mutageneses, the latter directed to two Ile
residues that play an important role in DNA recognition and bending by HMG
domains. The mutants were characterized in terms of their ability to
repress the hypoxic gene ANB1 and the auto-repressed ROX1 gene in vivo. The
mutant HMG domains were fused to maltose binding protein and expressed in
and purified from Escherichia coli and their relative affinities for DNA
and ability to bend DNA were determined. A model of the structure of the
Rox1 HMG domain was derived using sequence similarities between Rox1 and
the human protein SRY, the structure of which has been determined. The
results of the mutational analysis are interpreted in terms of the model
structure of Rox1.
ARTICLES
Characterization of the DNA binding and bending HMG domain of the yeast hypoxic repressor Rox1
Department of Biological Sciences, University at Albany/SUNY, Albany, NY 12222, USA.
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