Holliday junctions cleaved by Rad1?
Article Abstract:
Analysis of the interaction of Saccharomyces cerevisiae Rad1 protein with synthetic Holliday junctions by using junctions comprising a 12-base-pair homology domain shows the occurrence of endonucleolytic nicking in the central region of the DNA substrate, cleaving into products that migrate with a duplex marker. This duplex DNA shows a single-stranded behavior, which is suggestive of base-pair breathing. Hence the role of the Rad1 protein in cleaving the Holliday junction requires in-depth examination.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1995
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DNA helicases get physical
Article Abstract:
The PcrA helicase is isolated from Bacillus stearothermophilus and is involved in the replication, repair, recombination and transcription of DNA. The protein comprises of two domains, each of which contain two subdomains. The A subdomain of the PcrA helicase is structurally similar to that of the ATPase domain of the RecA protein of the Escherichia coli. The RecA protein is important for genetic recombination and DNA repair.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1996
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Structure of a multisubunit complex that promotes DNA branch migration
Article Abstract:
A new molecular model for the process of branch migration exhibited by two oppositely oriented RuvB ring motors is proposed. The model provides information the functioning of RuvA and RuvB proteins in the Escherichia coli. The RuvB is found to enhance the branch migration process and the RuvA binds all the Holliday junctions. The RuvB and RuvA are actively involved in the DNA repairing processes.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1995
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