Site-specific recognition of the bacteriophage Mu ends by the Mu A protein.
about
The Mu transpososome structure sheds light on DDE recombinase evolutionConformational isomerization in phage Mu transpososome assembly: effects of the transpositional enhancer and of MuB.Insertion sequencesArrayed transposase-binding sequences on the ends of transposon Tn5090/Tn402Mutational analysis of insertion sequence 50 (IS50) and transposon 5 (Tn5) endsAction at a distance in Mu DNA transposition: an enhancer-like element is the site of action of supercoiling relief activity by integration host factor (IHF).Bacteriophage Mu sites required for transposition immunity.The AAA+ ClpX machine unfolds a keystone subunit to remodel the Mu transpososome.Identification and purification of a Drosophila protein that binds to the terminal 31-base-pair inverted repeats of the P transposable element.3D reconstruction of the Mu transposase and the Type 1 transpososome: a structural framework for Mu DNA transposition.In vitro maturation and encapsidation of the DNA of transposable Mu-like phage D108.Studies on a "jumping gene machine": higher-order nucleoprotein complexes in Mu DNA transposition.The phiX174-type primosome promotes replisome assembly at the site of recombination in bacteriophage Mu transpositionSolution structure of the Mu end DNA-binding ibeta subdomain of phage Mu transposase: modular DNA recognition by two tethered domains.The cloning and characterization of the bacteriophage D108 regulatory DNA-binding protein nerPackaging specific segments of the Salmonella chromosome with locked-in Mud-P22 prophages.C-terminal deletions can suppress temperature-sensitive mutations and change dominance in the phage Mu repressor.Dynamics of a protein polymer: the assembly and disassembly pathways of the MuB transposition target complex.Identification of a transposon Tn7-dependent DNA-binding activity that recognizes the ends of Tn7.Specific binding of transposase to terminal inverted repeats of transposable element Tn3B protein of bacteriophage mu is an ATPase that preferentially stimulates intermolecular DNA strand transferStructural domains in phage Mu transposase: identification of the site-specific DNA-binding domainAltering the DNA-binding specificity of Mu transposase in vitro.Mutational analysis of the att DNA-binding domain of phage Mu transposaseCrucial role for DNA supercoiling in Mu transposition: a kinetic study.(+)-CC-1065 as a structural probe of Mu transposase-induced bending of DNA: overcoming limitations of hydroxyl-radical footprintingDNA binding activities of the Herves transposase from the mosquito Anopheles gambiae.Organization and dynamics of the Mu transpososome: recombination by communication between two active sites.Regulatory factors acting at the bacteriophage Mu middle promoter.Central location of the Mu strong gyrase binding site is obligatory for optimal rates of replicative transposition.ClpX protein of Escherichia coli activates bacteriophage Mu transposase in the strand transfer complex for initiation of Mu DNA synthesis.DNA-protein complexes during attachment-site synapsis in Mu DNA transposition.Structural aspects of a higher order nucleoprotein complex: induction of an altered DNA structure at the Mu-host junction of the Mu type 1 transpososomeDeciphering the Roles of Multicomponent Recognition Signals by the AAA+ Unfoldase ClpX.Autoregulation of phage mu transposase at the level of translationDNA sequence of the control region of phage D108: the N-terminal amino acid sequences of repressor and transposase are similar both in phage D108 and in its relative, phage Mu.Involvement of Escherichia coli FIS protein in maintenance of bacteriophage mu lysogeny by the repressor: control of early transcription and inhibition of transpositionDNA sequence of the E. coli gyrB gene: application of a new sequencing strategy.Specificity of mini-Mu bacteriophage insertions in a small plasmid.Characterization of the C operon transcript of bacteriophage Mu.
P2860
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P2860
Site-specific recognition of the bacteriophage Mu ends by the Mu A protein.
description
1984 nî lūn-bûn
@nan
1984年の論文
@ja
1984年学术文章
@wuu
1984年学术文章
@zh
1984年学术文章
@zh-cn
1984年学术文章
@zh-hans
1984年学术文章
@zh-my
1984年学术文章
@zh-sg
1984年學術文章
@yue
1984年學術文章
@zh-hant
name
Site-specific recognition of the bacteriophage Mu ends by the Mu A protein.
@en
Site-specific recognition of the bacteriophage Mu ends by the Mu A protein.
@nl
type
label
Site-specific recognition of the bacteriophage Mu ends by the Mu A protein.
@en
Site-specific recognition of the bacteriophage Mu ends by the Mu A protein.
@nl
prefLabel
Site-specific recognition of the bacteriophage Mu ends by the Mu A protein.
@en
Site-specific recognition of the bacteriophage Mu ends by the Mu A protein.
@nl
P2093
P1433
P1476
Site-specific recognition of the bacteriophage Mu ends by the Mu A protein.
@en
P2093
P304
P356
10.1016/0092-8674(84)90017-5
P407
P433
P577
1984-12-01T00:00:00Z