Structure of the bacteriophage Mu transposase core: a common structural motif for DNA transposition and retroviral integration
Article Abstract:
The crystal structure of the main domain of bacteriophage Mu transposase, MuA measured at 2.4 angstrom resolution reveals that the first of the two subdomains carries the active site. Despite extremely restricted homology reflecting a similarity, performing this experiment reveals a similarity to the core domain of HIV-1 integrase, which conducts a similar set of biochemical reactions. It also shows more restricted similarity to other nucleases, RNase H and Ruvc.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1995
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Mu transpositional recombination: donor DNA cleavage and strand transfer in trans by the Mu transposase
Article Abstract:
Donor DNA cleavage and strand transfer during Mu transpositional recombination take place only after the two ends of the Mu genome are synapsed by a MuA tetramer transposase. Phage Mu transposase MuA free in solution exists predominantly as a monomer that appears to catalytically inactive. Mu end synapsis, coupled with MuA tetramer formation, induces a structural transition that changes the MuA active site from the inactive to the active configuration.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1996
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Assembly of phage Mu transpososomes: cooperative transitions assisted by protein and DNA scaffolds
Article Abstract:
The assembly of phage Mu transpososomes occurs through two pathways, namely the internal activation sequence (IAS) pathway and the Mu transposase (Mu) B protein-target DNA complex pathway. The pathways necessitate the interaction of the four monomers of MuA with an assembly-assisting element such as IAS or MuB. The complexes with protein and DNA are essential for the initiation of transcription, recombination and replication.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1995
User Contributions:
Comment about this article or add new information about this topic:
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