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Competitive binding of MatP and topoisomerase IV to the MukB hinge domain

Gemma Lm Fisher1, Jani R Bolla2,3, Karthik V Rajasekar1

  • 1Department of Biochemistry, University of Oxford, Oxford, United Kingdom.

Elife
|September 29, 2021
PubMed

Insights

Structural Maintenance of Chromosomes (SMC) complexes like E. coli MukBEF are regulated by competitive binding. MatP and ParC bind mutually exclusively to the MukB hinge, controlling MukBEF distribution and function.

Area of Science:

  • Molecular Biology
  • Genetics
  • Microbiology

Background:

  • Structural Maintenance of Chromosomes (SMC) complexes are crucial for DNA compaction and chromosome organization.
  • In E. coli, the MukBEF complex plays a vital role in chromosome segregation.
  • MukBEF localization is regulated by interactions within the chromosome.

Purpose of the Study:

  • To investigate the interaction between MukBEF, MatP, and topoisomerase IV (ParC2E2).
  • To elucidate the mechanism of MukBEF depletion from the ter region.
  • To understand how competitive binding regulates MukBEF-ParC2E2 activity.

Main Methods:

  • Biochemical assays to study protein-protein and protein-DNA interactions.
  • Site-directed mutagenesis of the MukB hinge.
  • Analysis of bacterial cell phenotypes.

Main Results:

  • MatP and ParC bind to an overlapping interface on the MukB hinge in a mutually exclusive manner.
  • matS DNA competes with the MukB hinge for MatP binding.
  • Mutations at the ParC/MatP binding interface impair ParC binding and affect MukBEF function.

Conclusions:

  • Competitive binding between MatP and ParC at the MukB hinge is a key regulatory mechanism.
  • This mechanism controls the spatial and temporal activity of MukBEF and topoisomerase IV.
  • Regulation of MukBEF distribution is essential for chromosome segregation and cell viability.
Keywords:
E. coliMatPMukBEFSMCbiochemistrychemical biologychromosomechromosomesgene expressiontopoisomerase IV

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