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J Biol Chem, Vol. 273, Issue 10, 5520-5527, March 6, 1998
From the Department of Biological Chemistry, Faculty of
Biochemistry, The Weizmann Institute of Science, Rehovot 76100, Israel
The MucA and MucB proteins are plasmid-encoded
homologues of the Escherichia coli UmuD and UmuC proteins,
respectively. These proteins are required for SOS mutagenesis, although
their mechanism of action is unknown. By using the yeast two-hybrid
system we have discovered that MucB interacts with SSB, the single
strand DNA binding protein (SSB) of E. coli. To examine the
interaction at the protein level, the MucA, MucA', and MucB proteins
were overproduced, purified in denatured state, and refolded. Purified MucA and MucA' each formed homodimers, whereas MucB was a monomer under
native conditions. RecA promoted the cleavage of MucA to MucA', and
MucB was found to bind single-stranded DNA (ssDNA), similarly to the
properties of the homologous UmuD and UmuC proteins. Purified MucB
caused a shift in the migration of SSB in a sucrose density gradient,
consistent with an interaction between these proteins. Addition of MucB
to SSB-coated ssDNA caused increased electrophoretic mobility of the
nucleoprotein complex and increased staining of the DNA by ethidium
bromide. Analysis of radiolabeled SSB in the complexes revealed that
only a marginal release of SSB occurred upon addition of MucB. These
results suggest that MucB induces a major conformational change in the
SSB·ssDNA complex but does not promote massive release of SSB from
the DNA. The interaction with SSB might be related to the role of MucB
in SOS-regulated mutagenesis.
The Mutagenesis Protein MucB Interacts with Single Strand DNA
Binding Protein and Induces a Major Conformational Change in Its
Complex with Single-stranded DNA
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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