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Exploring human sperm nuclear basic protein-DNA interactions: could hexavalent chromium play an interfering role?

Gennaro Lettieri1, Carmen Di Giovanni2, Simona Amore1

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Hexavalent chromium disrupts sperm function by impairing sperm nuclear basic protein (SNBP) DNA binding, primarily through arginine modification. This highlights the critical role of arginine integrity in male reproductive health.

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Area of Science:

  • Biochemistry
  • Reproductive Biology
  • Toxicology

Background:

  • Sperm nuclear basic proteins (SNBP), mainly protamines, are crucial for DNA packaging and male fertility.
  • Arginine residues in SNBP mediate DNA interaction via salt bridges.
  • Hexavalent chromium [Cr(VI)] is a known reproductive toxicant.

Purpose of the Study:

  • To investigate the impact of Cr(VI) on SNBP-DNA binding.
  • To elucidate the role of arginine integrity in SNBP-DNA interactions under chromium exposure.
  • To understand the molecular mechanisms of chromium-induced reproductive toxicity.

Main Methods:

  • Electrophoretic mobility shift assays (EMSA) to assess SNBP-DNA complex formation.
  • SDS-PAGE and native-PAGE to analyze SNBP aggregation.
  • Fluorescence spectroscopy to study surface polar exposition changes.
  • Deguanidination of SNBP with hydrazine.
  • In silico molecular docking to model Cr(III)-arginine and Cr(III)-DNA interactions.

Main Results:

  • Cr(VI) treatment significantly impaired SNBP-DNA complex formation and induced SNBP aggregation.
  • Deguanidination of SNBP mimicked Cr(VI) effects on DNA binding.
  • Cr(III) forms coordination complexes with arginine guanidinium groups, disrupting DNA binding.
  • Cr(III) exhibits preferential binding to guanine in GC-rich DNA sequences.

Conclusions:

  • Arginine integrity is essential for proper SNBP-DNA binding and sperm chromatin organization.
  • Cr(VI)-induced genotoxicity in sperm is mediated by its reduced form, Cr(III), binding to arginine residues.
  • Disruption of SNBP-DNA binding by chromium affects human reproductive health.