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(Received for publication, April 28, 1997)
From the Institute of Cell and Molecular Biology, University of
Edinburgh, Kings Buildings, Edinburgh EH9 3JR, United Kingdom
The sbcC and sbcD genes
mediate palindrome inviability in Escherichia coli. The
sbcCD operon has been cloned into the plasmid pTrc99A under
the control of the strong trc promoter and introduced into
a strain carrying a chromosomal deletion of sbcCD. The SbcC and SbcD polypeptides were overexpressed to 6% of total cell protein, and both polypeptides copurified in a four-step purification procedure. Purified SbcCD is a processive double-strand exonuclease that has an
absolute requirement for Mn2+ and uses ATP as a preferred
energy source. Gel filtration chromatography and sedimentation
equilibrium analyses were used to show that the SbcC and SbcD
polypeptides dissociate at some stage after purification and that this
dissociation is reversed by the addition of Mn2+. We
demonstrate that SbcD has the potential to form a secondary structural
motif found in a number of protein phosphatases and suggest that it is
a metalloprotein that contains the catalytic center of the SbcCD
exonuclease.
Volume 272, Number 32,
Issue of August 8, 1997
pp. 19819-19826
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
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