Crystal structure of the replication terminator protein from B. subtilis at 2.6 angstrom
Article Abstract:
Analysis of the crystal structure of the replication terminator protein (RTP) of Bacillus subtilis at 2.6 angstrom resolution helps study replication termination at the molecular level. The molecule that belongs to the alpha+beta protein-folding class is a symmetric dimer, and is characterized by an alpha-helix and a beta-ribbon that interact with the minor and major grooves of B-DNA and an antiparallel coiled-coil that acts as the dimerization domain. RTP surface contains a site that is positionally and biochemically ideal for interaction with replication-specific helicase.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1995
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A 27 kd protein of E. coli promotes antitermination of replication in vitro at a sequence-specific replication terminus
Article Abstract:
The Escherichia coli ter protein is a tau-site binding protein that exhibits both polarized contrahelicase and replication fork-arresting activities. The interactions of ter with other cellular proteins and their effects on ter activities were investigated. The results showed that a 27-kd antiterminator (anti-ter) protein is capable of abolishing ter's contrahelicase and replication fork-arresting activities in vitro. It is proposed that ter and anti-ter interactions comprise a major regulatory mechanism for the termination of DNA replication.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1993
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Helicase-contrahelicase interaction and the mechanism of termination of DNA replication
Article Abstract:
Two alternative models for elucidating the mechanism of action of the replication terminator proteins are proposed. The steric hindrance model suggests that the complex between the terminator proteins and the terminator DNA sets up a polar, steric barrier to fork movement. The other model triggers a specific interaction between the terminator protein and the replicative helicase. Evidence strongly supports the second model.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1996
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