U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination
    • Showing Current items.

    mukB chromosome partitioning protein MukB [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 945549, updated on 3-Dec-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Intersubunit and intrasubunit interactions driving the MukBEF ATPase.

    Intersubunit and intrasubunit interactions driving the MukBEF ATPase.
    Bahng S, Kumar R, Marians KJ., Free PMC Article

    07/2/2022
    Acyl carrier protein promotes MukBEF action in Escherichia coli chromosome organization-segregation.

    Acyl carrier protein promotes MukBEF action in Escherichia coli chromosome organization-segregation.
    Prince JP, Bolla JR, Fisher GLM, Mäkelä J, Fournier M, Robinson CV, Arciszewska LK, Sherratt DJ., Free PMC Article

    01/1/2022
    Organization of the Escherichia coli Chromosome by a MukBEF Axial Core.

    Organization of the Escherichia coli Chromosome by a MukBEF Axial Core.
    Mäkelä J, Sherratt DJ., Free PMC Article

    08/15/2020
    Complex formation requires functional interactions between the C- and N-terminal domains of MukF with the MukB head and neck, respectively, and MukE, which organizes the complexes by stabilizing binding of MukB heads to MukF. In the absence of head engagement, a MukF dimer bound by MukE forms complexes containing only a dimer of MukB.

    Dynamic architecture of the Escherichia coli structural maintenance of chromosomes (SMC) complex, MukBEF.
    Rajasekar KV, Baker R, Fisher GLM, Bolla JR, Mäkelä J, Tang M, Zawadzka K, Koczy O, Wagner F, Robinson CV, Arciszewska LK, Sherratt DJ., Free PMC Article

    12/7/2019
    The authors show that a 4-helix bundle adjacent to the MukF dimerisation domain interacts functionally with the MukB coiled-coiled 'neck' adjacent to the ATPase head. They propose that this interaction leads to an asymmetric tripartite complex, as in other SMC (Structural Maintenance of Chromosomes) complexes.

    MukB ATPases are regulated independently by the N- and C-terminal domains of MukF kleisin.
    Zawadzka K, Zawadzki P, Baker R, Rajasekar KV, Wagner F, Sherratt DJ, Arciszewska LK., Free PMC Article

    08/17/2019
    Study reports that MukB binds topologically to DNA in vitro, and this binding is preferentially single-stranded DNA (ssDNA) rather than double-stranded DNA. The binding of MukB to ssDNA does not require ATP but the thermal energy enhances the binding.

    In vitro topological loading of bacterial condensin MukB on DNA, preferentially single-stranded DNA rather than double-stranded DNA.
    Niki H, Yano K., Free PMC Article

    07/14/2018
    MukB hinge region binds DNA and that this region of the protein is involved in sequestration of supercoils. Cells carrying mutations in the MukB hinge that reduce DNA condensation in vitro exhibit nucleoid decondensation in vivo.

    The bacterial condensin MukB compacts DNA by sequestering supercoils and stabilizing topologically isolated loops.
    Kumar R, Grosbart M, Nurse P, Bahng S, Wyman CL, Marians KJ., Free PMC Article

    10/21/2017
    Cells carrying a mukB mutant allele that encodes a protein that does not interact with topoisomerase IV exhibit severe nucleoid decompaction leading to chromosome segregation defects. These findings suggest that the MukB-topoisomerase IV complex may provide a scaffold for DNA condensation.

    The MukB-topoisomerase IV interaction is required for proper chromosome compaction.
    Kumar R, Nurse P, Bahng S, Lee CM, Marians KJ., Free PMC Article

    10/21/2017
    activity of MukB requires DNA binding by the head domains of the protein but does not require either ATP or its partner proteins MukE or MukF. The ability of MukB to mediate DNA catenation underscores its potential for bringing distal regions of a chromosome together.

    MukB-mediated Catenation of DNA Is ATP and MukEF Independent.
    Bahng S, Hayama R, Marians KJ., Free PMC Article

    05/27/2017
    MatP regulates the action of topoisomerase IV and MukBEF in chromosome segregation.

    MatP regulates the coordinated action of topoisomerase IV and MukBEF in chromosome segregation.
    Nolivos S, Upton AL, Badrinarayanan A, Müller J, Zawadzka K, Wiktor J, Gill A, Arciszewska L, Nicolas E, Sherratt D., Free PMC Article

    06/11/2016
    SecA defects are accompanied by dysregulation of MukB, gyrB, chromosome partitioning and DNA superhelicity.

    SecA defects are accompanied by dysregulation of MukB, DNA gyrase, chromosome partitioning and DNA superhelicity in Escherichia coli.
    Adachi S, Murakawa Y, Hiraga S.

    04/4/2015
    Taken together, the data implicate MukBEF as a key component of the DNA segregation process by acting in concert with TopoIV to promote decatenation and positioning of newly replicated oris.

    The SMC complex MukBEF recruits topoisomerase IV to the origin of replication region in live Escherichia coli.
    Nicolas E, Upton AL, Uphoff S, Henry O, Badrinarayanan A, Sherratt D., Free PMC Article

    08/30/2014
    MukB-ParC interaction may play a role in chromosome organization rather than in separation of daughter chromosomes

    The MukB-ParC interaction affects the intramolecular, not intermolecular, activities of topoisomerase IV.
    Hayama R, Bahng S, Karasu ME, Marians KJ., Free PMC Article

    05/18/2013
    MukBEF complexes may undergo multiple cycles of ATP hydrolysis without being released from DNA, analogous to the behavior of well-characterized molecular motors.

    In vivo architecture and action of bacterial structural maintenance of chromosome proteins.
    Badrinarayanan A, Reyes-Lamothe R, Uphoff S, Leake MC, Sherratt DJ., Free PMC Article

    11/24/2012
    findings show here that MukBEF generates and maintains the cellular positioning of chromosome loci independently of DNA replication.

    The Escherichia coli SMC complex, MukBEF, shapes nucleoid organization independently of DNA replication.
    Badrinarayanan A, Lesterlin C, Reyes-Lamothe R, Sherratt D., Free PMC Article

    11/3/2012
    Competing MukB-MukE and MukE-MukE interactions may regulate the formation of higher-order structures of bacterial condensin.

    The role of MukE in assembling a functional MukBEF complex.
    Gloyd M, Ghirlando R, Guarné A., Free PMC Article

    12/3/2011
    Using these experimental constraints, phylogenetic data, and coiled-coil prediction algorithms, the authors propose a pairing scheme for the discontinuous segments in the coiled coil.

    Identification of interacting regions within the coiled coil of the Escherichia coli structural maintenance of chromosomes protein MukB.
    Li Y, Weitzel CS, Arnold RJ, Oakley MG.

    01/21/2010
    Stable association of MukB with the chromosome required MukEF.

    MukEF Is required for stable association of MukB with the chromosome.
    She W, Wang Q, Mordukhova EA, Rybenkov VV., Free PMC Article

    01/21/2010
    In mukB mutant cells, the two chromosome arms do not separate into distinct cell halves, but extend from pole to pole with the oriC region located at the old pole.

    MukB colocalizes with the oriC region and is required for organization of the two Escherichia coli chromosome arms into separate cell halves.
    Danilova O, Reyes-Lamothe R, Pinskaya M, Sherratt D, Possoz C., Free PMC Article

    01/21/2010
    N-terminus verified by Edman degradation on complete protein

    E.coli MukB protein involved in chromosome partition forms a homodimer with a rod-and-hinge structure having DNA binding and ATP/GTP binding activities.
    Niki H, Imamura R, Kitaoka M, Yamanaka K, Ogura T, Hiraga S., Free PMC Article

    11/5/2007
    MukB has a unique set of topological properties, compared with other SMC proteins, and is likely to exist in two different conformations

    DNA reshaping by MukB. Right-handed knotting, left-handed supercoiling.
    Petrushenko ZM, Lai CH, Rai R, Rybenkov VV., Free PMC Article

    01/21/2010
    The positioning of replication forks is affected by the disruption of the mukB gene.

    Localization of replication forks in wild-type and mukB mutant cells of Escherichia coli.
    Adachi S, Kohiyama M, Onogi T, Hiraga S.

    01/21/2010
    firstprevious page of 1 nextlast