Dynamics of a protein polymer: The assembly and disassembly pathways of the MuB transposition target complex

EMBO Journal

Volumn 21, Issue 6, 2002, Pages 1477-1486

  Greene, Eric C ^a   Mizuuchi, Kiyoshi ^a  

^a NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES   (United States)

Author keywords

DNA transposition; Fluorescence resonance energy transfer; Green fluorescent protein; MuB

Indexed keywords

BACTERIAL PROTEIN; GREEN FLUORESCENT PROTEIN; POLYMER; PROTEIN MUB; UNCLASSIFIED DRUG;

ARTICLE; BACTERIAL GENOME; BACTERIOPHAGE; CHROMOSOME; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; DNA TRANSPOSITION; ENERGY TRANSFER; ESCHERICHIA COLI; GENE INSERTION; GENE TARGETING; HYDROLYSIS; MOLECULAR DYNAMICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN ASSEMBLY;

ADENOSINE TRIPHOSPHATE; BACTERIOPHAGE MU; DNA; DNA-BINDING PROTEINS; GREEN FLUORESCENT PROTEINS; HYDROLYSIS; KINETICS; LUMINESCENT PROTEINS; POLYMERS; PROMOTER REGIONS (GENETICS); RECOMBINANT FUSION PROTEINS; SPECTROMETRY, FLUORESCENCE; TRANSPOSASES; VIRAL PROTEINS;

BACTERIA (MICROORGANISMS); ENTEROBACTERIA PHAGE MU; ESCHERICHIA COLI; INSERTION SEQUENCES; NEGIBACTERIA; UNIDENTIFIED BACTERIOPHAGE;

EID: 0037086543     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/21.6.1477     Document Type: Article

References (24)

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2. Interaction of proteins located at a distance along DNA - Mechanism of target immunity in the Mu DNA strand-transfer reaction
3. Steady-state kinetic-analysis of ATP hydrolysis by the B-protein of bacteriophage-Mu - Involvement of protein oligomerization in the ATPase cycle
4. DNA-promoted assembly of the active tetramer of the Mu-transposase
5. MuB protein allosterically activates strand transfer by the transposase of phage-Mu
6. Division-of-labor among monomers within the Mu-transposase tetramer
7. A truncated form of the bacteriophage-Mu-B Protein promotes conservative integration, but not replicative transposition, of Mu-DNA
8. DNA transposition: Jumping gene machine, some assembly required
9. Target site selection in transposition
10. Transposition of Mu-DNA - Joining of Mu to target DNA can be uncoupled from cleavage at the ends of Mu
11. Site-specific recognition of the bacteriophage-Mu ends by the Mu-A protein
12. The solution structure of the C-terminal domain of the Mu-B transposition protein
13. B-protein of bacteriophage Mu is an ATPase that preferentially stimulates intermolecular DNA strand transfer
14. Monitoring protein conformations and interactions by fluorescence resonance energy transfer between mutants of green fluorescent protein
15. Transpositional recombination - Mechanistic insights from studies of Mu and other elements
16. Assembly of the active form of the transposase-Mu DNA complex - A critical control point in Mu-transposition
17. A new set of Mu DNA transposition intermediates: Alternate pathways of target capture preceding strand transfer
18. Stimulation of the Mu-DNA strand cleavage and intramolecular strand transfer-reactions by the Mu-B-protein is independent of stable binding of the Mu-B-protein to DNA
19. Transpososomes - Stable protein DNA complexes involved in the in vitro transposition of bacteriophage-Mu-DNA
20. Structure-function-relationships in the transposition protein-B of bacteriophage-Mu
21. Three-site synapsis during Mu DNA transposition: A critical intermediate preceding engagement of the active site
22. Organization and dynamics of the Mu transpososome: Recombination by communication between two active sites
23. Characterization of a region in phage Mu transposase that is involved in interaction with the Mu-B protein
24. An ATP-ADP switch in MuB controls progression of the Mu transposition pathway