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Replication terminator protein

FieldValue
SymbolRTP
NameReplication terminator protein
PfamPF02334
InterProIPR003432
SCOP1bm9

The replication terminator protein (RTP) is a DNA-binding protein that helps terminate DNA replication in Bacillus. It has a winged-helix structure and forms a homodimer via hydrogen bonds. The dimer is symmetric when it is not bound to DNA, but becomes asymmetrical when it is bound. Its termination activity is polar: it stops the replication fork from continuing in one direction, but a fork going the other direction is allowed to proceed.

Binding site

Each RTP dimer binds to a binding site 20 bp long. A ter site on the actual bacterial chromosome consists of two dimer-binding sites "A" and "B", with 3 bp of overlap. The "A" site matches the preference of RTP better and hence has higher affinity. Binding of the "A" site with an RTP dimer changes the shape of the "B" site such that it is easier to bind to another RTP dimer.

Mechanism

Before 2006, it was assumed that RTP simply terminates DNA replication by clamping onto the DNA and physically blocking the replication fork. In 2006, a study found that the contact between RTP and the DNA replication machinery likely also plays a role.

References

References

  1. (1 March 2001). "Structure of the RTP–DNA complex and the mechanism of polar replication fork arrest". Nature Structural Biology.
  2. (July 2007). "An Asymmetric Structure of the Bacillus subtilis Replication Terminator Protein in Complex with DNA". Journal of Molecular Biology.
  3. (August 2006). "DNA Replication Fork Arrest by the Bacillus subtilis RTP–DNA Complex Involves a Mechanism that Is Independent of the Affinity of RTP–DNA Binding". Journal of Molecular Biology.
Wikipedia Source

This article was imported from Wikipedia and is available under the Creative Commons Attribution-ShareAlike 4.0 License. Content has been adapted to SurfDoc format. Original contributors can be found on the article history page.

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