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J Biol Chem, Vol. 273, Issue 33, 20960-20966, August 14, 1998
From the Department of Chemistry, Princeton University, Princeton,
New Jersey 08544-1009 and the § Bristol-Myers Squibb
Pharmaceutical Research Institute,
Princeton, New Jersey 08543-4000
The protein WrbA had been identified as an
Escherichia coli stationary-phase protein that copurified
and coimmunoprecipitated with the tryptophan repressor. Sequences
homologous to WrbA have been reported in several species of yeast and
plants. We previously showed that this new family of proteins displays
low but structurally significant sequence similarity with flavodoxins
and that its members are predicted to share the
Biochemical Characterization of WrbA, Founding Member of a New
Family of Multimeric Flavodoxin-like Proteins
/
core of the
flavodoxin fold but with a short conserved insertion unique to the new
family, which could account for reports that some family members may be dimeric in solution. The general sequence similarity to flavodoxins suggests that the members of the new family might bind FMN, but their
wide evolutionary distribution indicates that, unlike the flavodoxins,
these proteins may be ubiquitous. In this paper, we report the
purification and biochemical characterization of WrbA, demonstrating
that the protein binds FMN specifically and is a multimer in solution.
The FMN binding constant is weaker than for many flavodoxins, being
~2 µM at 25 °C in 0.1 mM sodium phosphate, pH 7.2. The protein participates in a dimer-tetramer equilibrium over a wide range of solution conditions, with a midpoint at approximately 1.4 µM. One FMN binds per monomer and
has no apparent effect on the multimerization equilibrium. WrbA has no effect on the affinity or mode of DNA binding by the tryptophan repressor; thus, its physiological role remains unclear. Although many
proteins with flavodoxin-like domains are known to be multimers, WrbA
is apparently the first characterized case in which multimerization is
associated directly with the flavodoxin-like domain itself.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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