Nucleic Acids Research, Vol 27, Issue 4 1039-1046, Copyright © 1999 by Oxford University Press
JC Connelly, ES de Leau and DR Leach
The SbcCD protein is a member of a group of nucleases found in
bacteriophage T4 and T5, eubacteria, archaebacteria, yeast, Drosophila,
mouse and man. Evidence from electron microscopy has revealed a distinctive
structure consisting of two globular domains linked by a long region of
coiled coil, similar to that predicted for the members of the SMC family.
That a nuclease should have such an unusual structure suggests that its
mode of action may be complex. Here we show that the protein degrades
duplex DNA in a 3'-->5' direction. This degradation releases products
half the length of the original duplex suggesting simultaneous degradation
from two duplex ends. This may provide a link to the unusual structure of
the protein since our data are consistent with recognition and cleavage of
DNA ends followed by 3'- ->5' nicking by two nucleolytic centres within
a single nuclease molecule that releases a half length limit product. We
also show that cleavage is not simply at the point of a
single-strand/double-stand transition and that despite the dominant
3'-->5' polarity of degradation, a 5' single-strand can be cleaved when
attached to duplex DNA. The implications of this mechanism for the
processing of hairpins formed during DNA replication are discussed.
ARTICLES
DNA cleavage and degradation by the SbcCD protein complex from Escherichia coli
Institute of Cell and Molecular Biology, University of Edinburgh, Kings Buildings, Edinburgh EH9 3JR, UK.
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