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

Alexander Wolf, Monica Mantri, Astrid Heim, Udo Müller, Erika Fichter, Muhammad Mukram Mohamed Mackeen, Lothar Schermelleh, Gregory Dadie, Heinrich Leonhardt, Catherine Vénien-Bryan, Benedikt M. Kessler, Christopher J. Schofield, Angelika Böttger

Research output: Contribution to journalArticle

17 Citations (Scopus)

Abstract

Jmjd6 (jumonji-domain-containing protein 6) is an Fe(II)-and 2OG (2-oxoglutarate)-dependent oxygenase that catalyses hydroxylation of lysine residues in proteins involved in pre-mRNA splicing. Jmjd6 plays an essential role in vertebrate embryonic development and has been shown to modulate alternative splicing in response to hypoxic stress. In the present study we show that an alternatively spliced version of Jmjd6 lacking the polyS (polyserine) domain localizes to the nucleolus, predominantly in the fibrillar centre. Jmjd6 with the polyS domain deleted also interacts with nucleolar proteins. Furthermore, co-immunoprecipitation experiments and F2H (fluorescent 2-hybrid) assays demonstrate that Jmjd6 homo-oligomerization occurs in cells. In correlation with the observed variations in the subnuclear distribution of Jmjd6, the structure of Jmjd6 oligomers in vitro changes in the absence of the polyS domain, possibly reflecting the role of the polyS domain in nuclear/nucleolar shuttling of Jmjd6.

Original languageEnglish
Pages (from-to)357-370
Number of pages14
JournalBiochemical Journal
Volume453
Issue number3
DOIs
Publication statusPublished - 1 Aug 2013

Fingerprint

2-Oxoglutarate 5-Dioxygenase Procollagen-Lysine
Mixed Function Oxygenases
Proteins
Oxygenases
polyserine
Protein Domains
RNA Precursors
Oligomerization
Hydroxylation
Alternative Splicing
Nuclear Proteins
Immunoprecipitation
Lysine
Embryonic Development
Vertebrates
Oligomers
Assays

Keywords

  • Fe(II)- and 2-oxoglutarate-dependent oxygenase
  • JmjC
  • Lysine hydroxylation
  • Nucleolus
  • Polyserine domain
  • Pre-mRNA splicing

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Cite this

The polyserine domain of the lysyl-5 hydroxylase Jmjd6 mediates subnuclear localization. / Wolf, Alexander; Mantri, Monica; Heim, Astrid; Müller, Udo; Fichter, Erika; Mohamed Mackeen, Muhammad Mukram; Schermelleh, Lothar; Dadie, Gregory; Leonhardt, Heinrich; Vénien-Bryan, Catherine; Kessler, Benedikt M.; Schofield, Christopher J.; Böttger, Angelika.

In: Biochemical Journal, Vol. 453, No. 3, 01.08.2013, p. 357-370.

Research output: Contribution to journalArticle

Wolf, A, Mantri, M, Heim, A, Müller, U, Fichter, E, Mohamed Mackeen, MM, Schermelleh, L, Dadie, G, Leonhardt, H, Vénien-Bryan, C, Kessler, BM, Schofield, CJ & Böttger, A 2013, 'The polyserine domain of the lysyl-5 hydroxylase Jmjd6 mediates subnuclear localization', Biochemical Journal, vol. 453, no. 3, pp. 357-370. https://doi.org/10.1042/BJ20130529
Wolf, Alexander ; Mantri, Monica ; Heim, Astrid ; Müller, Udo ; Fichter, Erika ; Mohamed Mackeen, Muhammad Mukram ; Schermelleh, Lothar ; Dadie, Gregory ; Leonhardt, Heinrich ; Vénien-Bryan, Catherine ; Kessler, Benedikt M. ; Schofield, Christopher J. ; Böttger, Angelika. / The polyserine domain of the lysyl-5 hydroxylase Jmjd6 mediates subnuclear localization. In: Biochemical Journal. 2013 ; Vol. 453, No. 3. pp. 357-370.
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