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ProteomicsIdentification of AcpP-MukB binding sites using cross-linking mass spectrometry
Structural Maintenance of Chromosomes (SMC) complexes contribute ubiquitously to chromosome organization-segregation. SMC proteins have a conserved architecture, with a dimerization hinge and an ATPase head domain separated by a long antiparallel intramolecular coiled-coil. Dimeric SMC proteins inte...
ORGANISM(S): Escherichia coli 
2021-11-25 | PXD026062 | Pride
Acpp Cross-linking mass spectrometry Mukb Structural maintenance of chromosomes 
UnknownThe MukB-topoisomerase IV interaction is required for proper chromosome compaction.
Not available
S-EPMC5641886 | biostudies-literature
UnknownEscherichia coli condensin MukB stimulates topoisomerase IV activity by a direct physical interaction.
Not available
S-EPMC2973889 | biostudies-literature
UnknownStructural basis for the MukB-topoisomerase IV interaction and its functional implications in vivo.
Not available
S-EPMC3832749 | biostudies-literature
GenomicsEscherichia coli K-12 strain:k12
MukB ChIP-seq on synchronized cells
PRJNA1024669 | ENA
UnknownInvolvement of the inner surface residues of bacterial SMC protein MukB in the ssDNA binding in vitro.
Not available
S-EPMC12820191 | biostudies-literature
UnknownThe crystal structure of the hinge domain of the Escherichia coli structural maintenance of chromosomes protein MukB.
Not available
S-EPMC4335309 | biostudies-literature
UnknownMukB ATPases are regulated independently by the N- and C-terminal domains of MukF kleisin.
Not available
S-EPMC5812716 | biostudies-literature
UnknownCompetitive binding of MatP and topoisomerase IV to the MukB hinge domain.
Not available
S-EPMC8523169 | biostudies-literature
UnknownIn vitro topological loading of bacterial condensin MukB on DNA, preferentially single-stranded DNA rather than double-stranded DNA.
Not available
S-EPMC4937444 | biostudies-literature
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