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Mycobacterial and Human Nitrobindins: Structure and Function.

Giovanna De Simone1, Alessandra di Masi1, Gian Marco Vita1

  • 1Dipartimento di Scienze, Università Roma Tre, Roma, Italy.

Antioxidants & Redox Signaling
|April 17, 2020
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Summary
This summary is machine-generated.

Nitrobindins (Nbs) are heme-proteins that bind nitric oxide and scavenge harmful peroxynitrite. These findings suggest Nbs play conserved roles in sensing nitric oxide and in antioxidant defense systems.

Keywords:
Homo sapiensMycobacterium tuberculosishemenitrobindinperoxynitritereactivitystructure

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Proteomics

Background:

  • Nitrobindins (Nbs) are conserved heme-proteins with largely unknown physiological roles.
  • They possess a solvent-exposed heme-Fe(III) atom, suggesting potential roles in redox reactions or ligand binding.

Purpose of the Study:

  • To investigate the structural and functional properties of ferric Mycobacterium tuberculosis Nb (Mt-Nb(III)) and Homo sapiens Nb (Hs-Nb(III)).
  • To compare these properties with other Nbs and related proteins like myoglobins.
  • To elucidate the cellular localization and potential physiological functions of Hs-Nb.

Main Methods:

  • Comparative analysis of Nb structures and functions.
  • Overexpression of Hs-Nb in human embryonic kidney 293 cells.
  • Investigation of nitric oxide and histamine binding.
  • Peroxynitrite scavenging assays.
  • Identification of nuclear localization sequences.

Main Results:

  • Mt-Nb(III), At-Nb(III), and Hs-Nb(III) selectively bind nitric oxide but show low reactivity toward histamine.
  • Hs-Nb localizes to the cytoplasm and nucleus, with a nuclear localization sequence identified.
  • Hs-Nb is the C-terminal domain of the nuclear protein THAP4, suggesting a role in modulating transcriptional activity.
  • Both Mt-Nb(III) and Hs-Nb(III) scavenge peroxynitrite and protect l-tyrosine from nitration.

Conclusions:

  • Nbs possess an evolutionarily conserved function as nitric oxide sensors and components of antioxidant systems.
  • Human THAP4 may couple heme-based Nb reactivity to gene transcription.
  • Mt-Nb(III) likely contributes to scavenging reactive nitrogen and oxygen species during host immune responses.