B protein of bacteriophage mu is an ATPase that preferentially stimulates intermolecular DNA strand transfer
about
The solution structure of the C-terminal domain of the Mu B transposition proteinMuB is an AAA+ ATPase that forms helical filaments to control target selection for DNA transpositionThe SET complex acts as a barrier to autointegration of HIV-1In vitro maturation and encapsidation of the DNA of transposable Mu-like phage D108.Avoiding self: two Tn7-encoded proteins mediate target immunity in Tn7 transposition.An ATP-ADP switch in MuB controls progression of the Mu transposition pathway.Gain-of-function mutations in TnsC, an ATP-dependent transposition protein that activates the bacterial transposon Tn7Target joining of duplicated insertion sequence IS21 is assisted by IstB protein in vitroPhage Mu transposition immunity: protein pattern formation along DNA by a diffusion-ratchet mechanism.Dynamics of a protein polymer: the assembly and disassembly pathways of the MuB transposition target complex.HIV DNA is heavily uracilated, which protects it from autointegrationPurification and characterization of TnsC, a Tn7 transposition protein that binds ATP and DNA.Retrotransposon suicide: formation of Ty1 circles and autointegration via a central DNA flap.ATPase activity of the UvrA and UvrAB protein complexes of the Escherichia coli UvrABC endonucleaseDNA-protein complexes during attachment-site synapsis in Mu DNA transposition.Transposons to toxins: the provenance, architecture and diversification of a widespread class of eukaryotic effectorsDeciphering the Roles of Multicomponent Recognition Signals by the AAA+ Unfoldase ClpX.Uncoupling of transpositional immunity from gamma delta transposition by a mutation at the end of gamma delta.Efficient autointegration of avian retrovirus DNA in vitro.Dissecting the roles of MuB in Mu transposition: ATP regulation of DNA binding is not essential for target deliveryAlternative interactions between the Tn7 transposase and the Tn7 target DNA binding protein regulate target immunity and transposition.Mechanisms of Evolution in High-Consequence Drug Resistance Plasmids.MuB gives a new twist to target DNA selection.Complete genomic sequence of bacteriophage B3, a Mu-like phage of Pseudomonas aeruginosa.The phage Mu transpososome core: DNA requirements for assembly and function.A domain sharing model for active site assembly within the Mu A tetramer during transposition: the enhancer may specify domain contributions.Heteromeric transposase elements: generators of genomic islands across diverse bacteria.Differential role of the Mu B protein in phage Mu integration vs. replication: mechanistic insights into two transposition pathways.Reorganization of the Mu transpososome active sites during a cooperative transition between DNA cleavage and joining.Sleeping Beauty transposition: from biology to applications.Towards integrating vectors for gene therapy: expression of functional bacteriophage MuA and MuB proteins in mammalian cells.Transposon Tn5090 of plasmid R751, which carries an integron, is related to Tn7, Mu, and the retroelementsInteractions of the transposase with the ends of Mu: formation of specific nucleoprotein structures and non-cooperative binding of the transposase to its binding sites.Transposase A binding sites in the attachment sites of bacteriophage Mu that are essential for the activity of the enhancer and A binding sites that promote transposition towards Fpro-lac.MuA-mediated in vitro cloning of circular DNA: transpositional autointegration and the effect of MuB.An Atypical AAA+ ATPase Assembly Controls Efficient Transposition through DNA Remodeling and Transposase Recruitment.Secondary structural features of the bacteriophage Mu-encoded A and B transposition proteins.Target DNA bending by the Mu transpososome promotes careful transposition and prevents its reversal.The dynamic Mu transpososome: MuB activation prevents disintegration.A new set of Mu DNA transposition intermediates: alternate pathways of target capture preceding strand transfer.
P2860
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P2860
B protein of bacteriophage mu is an ATPase that preferentially stimulates intermolecular DNA strand transfer
description
1987 nî lūn-bûn
@nan
1987 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1987 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1987年の論文
@ja
1987年論文
@yue
1987年論文
@zh-hant
1987年論文
@zh-hk
1987年論文
@zh-mo
1987年論文
@zh-tw
1987年论文
@wuu
name
B protein of bacteriophage mu ...... rmolecular DNA strand transfer
@en
B protein of bacteriophage mu ...... rmolecular DNA strand transfer
@nl
type
label
B protein of bacteriophage mu ...... rmolecular DNA strand transfer
@en
B protein of bacteriophage mu ...... rmolecular DNA strand transfer
@nl
prefLabel
B protein of bacteriophage mu ...... rmolecular DNA strand transfer
@en
B protein of bacteriophage mu ...... rmolecular DNA strand transfer
@nl
P2093
P2860
P356
P1476
B protein of bacteriophage mu ...... rmolecular DNA strand transfer
@en
P2093
P2860
P304
P356
10.1073/PNAS.84.3.699
P407
P577
1987-02-01T00:00:00Z