Nucleic Acids Research, Vol 25, Issue 3 590-596, Copyright © 1997 by Oxford University Press
AV Kralicek, PK Wilson, GB Ralston, RG Wake and GF King
Termination of DNA replication in Bacillus subtilis involves the polar
arrest of replication forks by a specific complex formed between the
replication terminator protein (RTP) and DNA terminator sites. While
determination of the crystal structure of RTP has facilitated our
understanding of how a single RTP dimer interacts with terminator DNA,
additional information is required in order to understand the assembly of a
functional fork arrest complex, which requires an interaction between two
RTP dimers and the terminator site. In this study, we show that the
conformation of the major B.subtilis DNA terminator,TerI, becomes
considerably distorted upon binding RTP. Binding of the first dimer of RTP
to the B site of TerI causes the DNA to become slightly unwound and bent by
approximately 40 degrees. Binding of a second dimer of RTP to the A site
causes the bend angle to increase to approximately 60 degrees . We have
used this new data to construct two plausible models that might explain how
the ternary terminator complex can block DNA replication in a polar manner.
In the first model, polarity of action is a consequence of the two RTP-DNA
half-sites having different conformations. These different conformations
result from different RTP- DNA contacts at each half-site (due to the
intrinsic asymmetry of the terminator DNA), as well as interactions (direct
or indirect) between the RTP dimers on the DNA. In the second model, polar
fork arrest activity is a consequence of the different affinities of RTP
for the A and B sites of the terminator DNA, modulated significantly by
direct or indirect interactions between the RTP dimers.
ARTICLES
Reorganization of terminator DNA upon binding replication terminator protein: implications for the functional replication fork arrest complex
Department of Biochemistry, University of Sydney, Sydney, NSW 2006, Australia.
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