Organization and dynamics of the Mu transpososome: recombination by communication between two active sites
Article Abstract:
The Mu transpososome and recombination by communication between two active sites are discussed relative to organization and dynamics. The recombination of the two Mu DNA ends where one active site promotes both cleavage and joining of one Mu DNA end has been shown to be catalyzed by two active sites. It has been proposed that the DNA joining stage must have a cooperative transition within the transposase-DNA complex. Cooperation in using active sites in trans by Mu transposase is an example of mobile elements ensuring concomitant recombination of distant DNA sites.
Publication Name: Genes & Development
Subject: Biological sciences
ISSN: 0890-9369
Year: 1999
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Tagging chromatin with retrotransposons: target specificity of the Saccharomyces Ty5 retrotransposon changes with the chromosomal localization of Sir3p and Sir4p
Article Abstract:
Tagging chromatin with retrotransposons is discussed relative to chromosomal localization of Sir3p and Sir4p and target specificity of Saccharomyces Ty5 retrotransposon changes. The model involving retroelement target specificity coming from recognition of specific chromatin components in integration has been studied with emphasis on Ty5 integration patterns in strains with deletions of individual SIR genes. Target specificity is largely gone in strains without Sir3p/Sir4p.
Publication Name: Genes & Development
Subject: Biological sciences
ISSN: 0890-9369
Year: 1999
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The interwoven architecture of the Mu transposase couples DNA synapsis to catalysis
Article Abstract:
The interwoven architecture of the Mu transposase couples DNA synapsis and tetramer assembly to catalysis during recombination. The Mu transposase tetramer binds the ends of the phage genome and carries out the two DNA cleavage and two DNA joining steps that transpose the Mu DNA to a new DNA site. End-type Mu binding sites contribute the active-site region from domain II and the essential functions in domain III during catalysis of strand transfer.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1996
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