(Q44456263)

3 December 2017

title

Mu transpososome architecture ensures that unfolding by ClpX or proteolysis by ClpXP remodels but does not destroy the complex (English)

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3 December 2017

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Briana M Burton

1

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3 December 2017

Tania A Baker

series ordinal

2

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3 December 2017

publication date

1 May 2003

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3 December 2017

number of pages

10

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inferred from page(s)

published in

Chemistry and Biology

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3 December 2017

volume

10

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3 December 2017

issue

5

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3 December 2017

page(s)

463-472

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Quality control in Mu DNA transposition

3 December 2017

cites work

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7 January 2021

Comparative architecture of transposase and integrase complexes

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7 January 2021

A defined system for the DNA strand-transfer reaction at the initiation of bacteriophage Mu transposition: protein and DNA substrate requirements

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7 January 2021

Molecular chaperones: clamps for the Clps?

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7 January 2021

New insights into the ATP-dependent Clp protease: Escherichia coli and beyond

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C-terminal extension of truncated recombinant proteins in Escherichia coli with a 10Sa RNA decapeptide.

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Role of a peptide tagging system in degradation of proteins synthesized from damaged messenger RNA

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7 January 2021

The structure of ClpP at 2.3 A resolution suggests a model for ATP-dependent proteolysis

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7 January 2021

ClpA mediates directional translocation of substrate proteins into the ClpP protease

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7 January 2021

Dynamics of substrate denaturation and translocation by the ClpXP degradation machine

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7 January 2021

Substrate recognition by the ClpA chaperone component of ClpAP protease

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7 January 2021

Protein binding and unfolding by the chaperone ClpA and degradation by the protease ClpAP.

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Scanning transmission electron microscopy and small-angle scattering provide evidence that native Escherichia coli ClpP is a tetradecamer with an axial pore.

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Endopeptidase Clp: ATP-dependent Clp protease from Escherichia coli

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7 January 2021

Global unfolding of a substrate protein by the Hsp100 chaperone ClpA.

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7 January 2021

ClpX-mediated remodeling of mu transpososomes: selective unfolding of subunits destabilizes the entire complex

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7 January 2021

A new component of bacteriophage Mu replicative transposition machinery: the Escherichia coli ClpX protein.

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7 January 2021

Transposition of Mu DNA: joining of Mu to target DNA can be uncoupled from cleavage at the ends of Mu.

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7 January 2021

Assembly of the active form of the transposase-Mu DNA complex: a critical control point in Mu transposition

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7 January 2021

Disassembly of the Bacteriophage Mu Transposase for the Initiation of Mu DNA Replication

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7 January 2021

Disassembly of the Mu transposase tetramer by the ClpX chaperone

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7 January 2021

ClpA and ClpP remain associated during multiple rounds of ATP-dependent protein degradation by ClpAP protease

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7 January 2021

The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging system

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7 January 2021

Versatile action of Escherichia coli ClpXP as protease or molecular chaperone for bacteriophage Mu transposition

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7 January 2021

DNase protection analysis of the stable synaptic complexes involved in Mu transposition

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7 January 2021

Division of labor among monomers within the Mu transposase tetramer

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7 January 2021

Identification of residues in the Mu transposase essential for catalysis

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7 January 2021

The mu transposase tetramer is inactive in unassisted strand transfer: an auto-allosteric effect of mu A promotes the reaction in the absence of mu B

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7 January 2021

Organization and dynamics of the Mu transpososome: recombination by communication between two active sites

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7 January 2021

Structure of the bacteriophage Mu transposase core: a common structural motif for DNA transposition and retroviral integration

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7 January 2021

The Mu three-site synapse: a strained assembly platform in which delivery of the L1 transposase binding site triggers catalytic commitment.

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7 January 2021

Kinetics of Mu DNA synthesis

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7 January 2021

The phiX174-type primosome promotes replisome assembly at the site of recombination in bacteriophage Mu transposition

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7 January 2021

NSF--fusion and beyond

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7 January 2021

A Structural Change Occurs upon Binding of Syntaxin to SNAP-25

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7 January 2021

The synaptic SNARE complex is a parallel four-stranded helical bundle

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7 January 2021

Recruitment of a 19S proteasome subcomplex to an activated promoter

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7 January 2021

A nonproteolytic function of the 19S regulatory subunit of the 26S proteasome is required for efficient activated transcription by human RNA polymerase II.

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7 January 2021

ClpX and MuB interact with overlapping regions of Mu transposase: implications for control of the transposition pathway.

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7 January 2021

Overlapping recognition determinants within the ssrA degradation tag allow modulation of proteolysis.

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7 January 2021

Sequence and positional requirements for DNA sites in a mu transpososome

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7 January 2021

B protein of bacteriophage mu is an ATPase that preferentially stimulates intermolecular DNA strand transfer

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7 January 2021

MuB protein allosterically activates strand transfer by the transposase of phage Mu

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7 January 2021

10.1016/S1074-5521(03)00102-9

Identifiers

DOI

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3 December 2017

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