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The polyserine domain of the lysyl-5 hydroxylase Jmjd6 mediates subnuclear localization

Alexander Wolf1, Monica Mantri, Astrid Heim

  • 1Institute of Molecular Toxicology and Pharmacology, Helmholtz Zentrum München-German Research Center for Environmental Health, Ingolstädter Landstrasse 1, 85764 Neuherberg, Germany.

The Biochemical Journal
|May 22, 2013
PubMed

Insights

The jumonji-domain-containing protein 6 (Jmjd6) protein

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Jmjd6 (jumonji-domain-containing protein 6) is an oxygenase crucial for pre-mRNA splicing and embryonic development.
  • Jmjd6's role in alternative splicing modulation under hypoxic stress is established.
  • The protein's subnuclear localization and oligomerization dynamics are not fully understood.

Purpose of the Study:

  • To investigate the impact of the polyserine (polyS) domain on Jmjd6's subnuclear localization and oligomerization.
  • To explore the functional consequences of Jmjd6 structural changes.

Main Methods:

  • Generation of Jmjd6 variants lacking the polyS domain.
  • Subcellular localization studies using microscopy.
  • Co-immunoprecipitation and fluorescent 2-hybrid (F2H) assays for protein interactions and homo-oligomerization.
  • In vitro analysis of Jmjd6 oligomer structure.

Main Results:

  • An alternatively spliced Jmjd6 variant lacking the polyS domain localizes to the nucleolus, specifically the fibrillar center.
  • Jmjd6 without the polyS domain interacts with nucleolar proteins.
  • Jmjd6 exhibits homo-oligomerization in cells.
  • The absence of the polyS domain alters Jmjd6 oligomer structure in vitro, potentially affecting nuclear/nucleolar shuttling.

Conclusions:

  • The polyS domain significantly influences Jmjd6's subnuclear localization and nucleolar interactions.
  • Jmjd6 homo-oligomerization is a key feature, with structural changes linked to the polyS domain.
  • These findings suggest a role for the polyS domain in regulating Jmjd6's nuclear-nucleolar transport and function.

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