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J. Biol. Chem., Vol. 276, Issue 6, 4447-4453, February 9, 2001
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Binds and Organizes Escherichia coli Replication
Proteins through Distinct Domains
AND 
, BINDS 
' AND 
*
From the Department of Biochemistry and Molecular Genetics and
Program in Molecular Biology, University of Colorado Health Sciences
Center, Denver, Colorado 80262
The DnaX complex of the DNA polymerase holoenzyme
assembles the 
2 processivity factor onto the
primed template enabling highly processive replication. The key ATPases
within this complex are and , alternative frameshift products of
the dnaX gene. Of the five domains of , I-III are
shared with In vivo, binds the auxiliary
subunits ' and (Glover, B. P., and McHenry, C. S. (2000) J. Biol. Chem. 275, 3017-3020). To localize
' and binding domains within domains I-III, we
measured the binding of purified biotin-tagged DnaX proteins lacking
specific domains to ' and by surface plasmon resonance.
Fusion proteins containing either DnaX domains I-III or domains III-V
bound ' and subunits. A DnaX protein only containing
domains I and II did not bind ' or . The binding affinity
of for DnaX domains I-III and domains III-V was the same as
that of for full-length , indicating that domain III
contained all structural elements required for binding. Domain
III of also contained ' binding sites, although the
interaction between ' and domains III-V of was 10-fold
weaker than the interaction between ' and full length . The
presence of both and strengthened the '-C(0)
interaction by at least 15-fold. Domain III was the only domain common
to all of fusion proteins whose interaction with ' was enhanced in the presence of and . Thus, domain III of the DnaX
proteins not only contains the ' and binding sites but
also contains the elements required for the positive cooperative
assembly of the DnaX complex.
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