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J. Biol. Chem., Vol. 276, Issue 38, 35842-35846, September 21, 2001
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Binds and Organizes Escherichia coli Replication
Proteins through Distinct Domains
AND 
, OLIGOMERIZES DnaX*
,
From the Department of Biochemistry and Molecular Genetics,
University of Colorado Health Sciences Center,
Denver, Colorado 80262
The and proteins of the DNA polymerase
III holoenzyme DnaX complex are products of the dnaX gene
with being a truncated version of arising from ribosomal
frameshifting. is comprised of five structural domains, the first
three of which are shared by (Gao, D., and McHenry, C. (2001)
J. Biol. Chem. 276, 4433-4453). In the absence of the
other holoenzyme subunits, DnaX exists as a tetramer. Association of
, ', 
, and 
with domain III of DnaX4 results in
a DnaX complex with a stoichiometry of DnaX3'. To identify which domain facilitates DnaX self-association, we examined
the properties of purified biotin-tagged DnaX fusion proteins
containing domains I-II or III-V. Unlike domain I-II, treatment of
domain III-V, , and with the chemical cross-linking reagent BS3
resulted in the appearance of high molecular weight intramolecular
cross-linked protein. Gel filtration of domains I-II and III-V
demonstrated that domain I-II was monomeric, and domain III-V was an
oligomer. Biotin-tagged domain III-V, and not domain I-II, was able to
form a mixed DnaX complex by recruiting , , ', , and onto streptavidin-agarose beads. Thus, domain III not only contains the
, ', , and binding interface, but also the region that
enables DnaX to oligomerize.
Present address: Dept. of Molecular and Cell Biology, University
of California, Berkeley, CA 94720.
§
To whom correspondence should be addressed: Dept. of Biochemistry
and Molecular Genetics, University of Colorado Health Sciences Center,
4200 East Ninth Ave., B121, Denver, CO 80262.
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