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J Biol Chem, Vol. 275, Issue 10, 6928-6936, March 10, 2000
From the Department of Biochemistry, School of Medical Sciences,
University of Bristol, University Walk,
Bristol, BS8 1TD, United Kingdom
Type II restriction enzymes generally recognize
continuous sequences of 4-8 consecutive base pairs on DNA, but some
recognize discontinuous sites where the specified sequence is
interrupted by a defined length of nonspecific DNA. To date, a
mechanism has been established for only one type II endonuclease with a
discontinuous site, SfiI at GGCCNNNNNGGCC (where N is any
base). In contrast to orthodox enzymes such as EcoRV,
dimeric proteins that act at a single site, SfiI is a
tetramer that interacts with two sites before cleaving DNA.
BglI has a similar recognition sequence (GCCNNNNNGGC) to SfiI but a crystal structure like EcoRV.
BglI and several other endonucleases with discontinuous
sites were examined to see if they need two sites for their DNA
cleavage reactions. The enzymes included some with sites containing
lengthy segments of nonspecific DNA, such as XcmI
(CCANNNNNNNNNTGG). In all cases, they acted at individual sites.
Elongated recognition sites do not necessitate unusual reaction
mechanisms. Other experiments on BglI showed that it bound
to and cleaved DNA in the same manner as EcoRV, thus
further delineating a distinct group of restriction enzymes with
similar structures and a common reaction mechanism.
Reactions of BglI and Other Type II Restriction
Endonucleases with Discontinuous Recognition Sites*
*
This work was supported by Grants 7/G10881 and 046178 from
the Biotechnology and Biological Sciences Research Council and the
Wellcome Trust.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.: 44-117-928-7429;
Fax: 44-117-928-8274; E-mail: s.halford@bris.ac.uk.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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