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The Escherichia coli replicase, DNA polymerase III
holoenzyme, derives its processivity from the
Volume 270,
Number 22,
Issue of June 2, pp. 13358-13365, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
II. INTERMEDIATE COMPLEX BETWEEN THE CLAMP LOADER AND ITS CLAMP
subunit sliding
clamp that encircles DNA and tethers the replicase to the template. The
dimer is assembled around DNA by the complex clamp loader
in an ATP-dependent reaction. In this report, the essential contact
between the clamp loader and
is identified as mediated through
the subunit of the
complex. The
subunit appears to
contact the face of the
dimer ring that contains the two C
termini. Surprisingly, ATP is required for the complex to bind
, but not for to bind
. This indicates that is
buried in the
complex and suggests a role for ATP in exposing
for interaction with
. A protease protection assay has been
developed to specifically probe the subunit within the
complex. The results of the assay are consistent with an ATP-induced
conformational change in the
complex that alters the state of the
subunit within it. The implication of these key features to the
clamp loading mechanism of the
complex is discussed.
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A. E. Pritchard and C. S. McHenry Assembly of DNA Polymerase III Holoenzyme. CO-ASSEMBLY OF gamma AND tau IS INHIBITED BY DnaX COMPLEX ACCESSORY PROTEINS BUT STIMULATED BY DNA POLYMERASE III CORE J. Biol. Chem., September 7, 2001; 276(37): 35217 - 35222. [Abstract] [Full Text] [PDF]
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B. P. Glover, A. E. Pritchard, and C. S. McHenry tau Binds and Organizes Escherichia coli Replication Proteins through Distinct Domains. DOMAIN III, SHARED BY gamma AND tau , OLIGOMERIZES DnaX J. Biol. Chem., September 14, 2001; 276(38): 35842 - 35846. [Abstract] [Full Text] [PDF]
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