Domain III function of Mu transposase analysed by directed placement of subunits within the transpososome

Journal of Biosciences

Volumn 25, Issue 4, 2000, Pages 347-360

  Mariconda, S ^a   Namgoong, S Y ^a   Yoon, K H ^a   Jiang, H ^a   Harshey, R M ^a  

^a UNIVERSITY OF TEXAS AT AUSTIN   (United States)

Author keywords

DNA transposition; MuA transposase; Phage Mu; Transpososome assembly

Indexed keywords

DNA BINDING PROTEIN; MU TRANSPOSASE; NUCLEASE; TRANSPOSASE; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; CATALYSIS; CONTROLLED STUDY; DNA SUPERCOILING; DNA TRANSPOSITION; ENZYME ANALYSIS; ENZYME SUBUNIT; HUMAN; HUMAN CELL; HUMAN TISSUE; PROTEIN DOMAIN; STRUCTURE ANALYSIS;

ENTEROBACTERIA PHAGE MU;

EID: 0034486638     PISSN: 02505991     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF02703788     Document Type: Article

References (40)

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2. Identification of residues in the Mu transposase essential for catalysis
3. MuB protein allosterically activates strand transfer by the transposase of phage Mu
4. The three chemical steps of Tn1O/IS1O transposition involve repeated utilization of a single active site
5. DNA transposition-jumping gene machine, some assembly required
6. DNA cleavage in trans by the active site tyrosine during Flp recombination: Switching protein partners before exchanging strands
7. Transposition of Mu DNA: Joining of Mu to target DNA can be uncoupled from cleavage at the ends of Mu
8. Three-dimensional structure of the Tn5 synaptic complex transposition intermediate
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10. Carboxyl-terminal mutants of phage Mu transposase
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13. Mutational analysis of the Mu transposase. Contributions of two distinct regions of domain II to recombination
14. ClpX protein of Escherichia coli activates bacteriophage Mu transposase in the strand transfer complex for initiation of Mu DNA synthesis
15. DNA-protein complexes during attachment-site synapsis in Mu DNA transposition
16. Transposition of phage Mu DNA
17. Two mutations of phage Mu transposase that affect strand transfer or interactions with B protein lie in distinct polypeptide domains
18. Disassembly of the Mu transposase tetramer by the ClpX chaperone
19. ClpX and MuB interact with overlapping regions of Mu transposase: Implications for control of the transposition pathway
20. Creation of phosphorylation sites in proteins: Construction of a phosphorylatable human interferon alpha
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22. Polynucleotidyl transfer reactions in transpositional DNA recombination
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24. Target site selection in transposition of phage Mu
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26. Structural domains in phage Mu transposase: Identification of the site-specific DNA-binding domain
27. The same two monomers within a MuA tetramer provide the DDE domains for the strand cleavage and strand transfer steps of transposition
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29. Mutational analysis of domain IIβ of bacteriophage Mu transposase: Domains IIα and IIβ belong to different catalytic complementation groups
30. Altering the DNA-binding specificity of Mu transposase in vitro
31. Structure of the bacteriophage Mu transposase core: A common structural motif for DNA transposition and retroviral integration
32. The Tn7 transposase is a heteromeric complex in which DNA breakage and joining activities are distributed between different gene products
33. Mu Transpositional Recombination: Donor DNA cleavage and strand transfer in trans by the Mu transposase
34. Stimulation of the Mu A protein-mediated strand cleavage reaction by the Mu B protein, and the requirement of DNA nicking for stable type 1 transpososome formation. In vitro transposition characteristics of mini-Mu plasmids carrying terminal base pair mutations
35. Three-site synapsis during Mu DNA transposition: A critical intermediate preceding engagement of the active site
36. Characterization of a region in phage Mu transposase that is involved in interaction with the Mu B protein
37. A novel DNA binding and nuclease activity in domain III of Mu transposase: Evidence for a catalytic region involved in donor cleavage
38. An ATP-ADP switch in MuB controls progression of the Mu transposition pathway
39. Positional information within the Mu transposase tetramer: Catalytic contributions of individual monomers
40. Domain sharing model for active site assembly within the Mu a tetramer during transposition: The enhancer may specify domain contributions