Structural and DNA binding properties of mycobacterial integration host factor mIHF

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Nina T Odermatt1, Moreno Lelli2, Torsten Herrmann3

  • 1École Polytechnique Fédérale de Lausanne, School of Life Sciences, Station 19, 1015 Lausanne, Switzerland.

Journal of Structural Biology
|December 18, 2019
PubMed

Insights

Mycobacterial integration host factor (mIHF) stabilizes DNA and introduces loops, aiding chromosome organization in Mycobacterium tuberculosis. This essential protein

Area of Science:

  • Microbiology
  • Structural Biology
  • Biochemistry

Background:

  • Nucleoid Associated Proteins (NAPs) are crucial for bacterial chromosome organization, DNA supercoiling, and gene regulation.
  • Mycobacterial integration host factor (mIHF) is an essential NAP in Mycobacterium tuberculosis, vital for its survival.

Purpose of the Study:

  • To characterize the biophysical and structural properties of mIHF.
  • To elucidate the DNA binding mechanism and DNA architectural changes induced by mIHF.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy for structural determination.
  • In vitro DNA binding assays.
  • Atomic Force Microscopy (AFM) for DNA looping visualization.

Main Results:

  • mIHF binding enhances protein stability and increases melting temperature.
  • NMR reveals mIHF as a rigid globular protein with a protruding alpha helix and disordered N-terminus.
  • mIHF binds double-stranded DNA via two distinct DNA binding sites and induces left-handed DNA loops, relaxing supercoiled DNA.

Conclusions:

  • mIHF possesses structural and DNA-binding characteristics similar to other IHF proteins.
  • mIHF plays a significant role in Mycobacterium tuberculosis DNA topology management and chromosome organization.
Keywords:
Atomic force microscopyDNA bindingMycobacterial integration host factorNMR structural determinationNucleoid associated proteinmIHF

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