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J Biol Chem. 2014 Dec 5;289(49):33999-4012. doi: 10.1074/jbc.M114.576785. Epub 2014 Oct 21.

Reptin and Pontin oligomerization and activity are modulated through histone H3 N-terminal tail interaction.

Author information

1
From the Laboratoire de Biologie Moléculaire Eucaryote, CNRS/UMR 5099, F-31062 Toulouse Cedex, the Université de Toulouse, UPS, 31062 Toulouse Cedex, and.
2
the Institut de Génétique et de Biologie Moléculaire et Cellulaire, CNRS/INSERM, Université de Strasbourg, 67404 Illkirch Cedex, France.
3
From the Laboratoire de Biologie Moléculaire Eucaryote, CNRS/UMR 5099, F-31062 Toulouse Cedex, the Université de Toulouse, UPS, 31062 Toulouse Cedex, and odile.humbert@ibcg.biotoul.fr.

Abstract

Pontin/RUVBL1 and Reptin/RUVBL2 are DNA-dependent ATPases involved in numerous cellular processes and are essential components of chromatin remodeling complexes and transcription factor assemblies. However, their existence as monomeric and oligomeric forms with differential activity in vivo reflects their versatility. Using a biochemical approach, we have studied the role of the nucleosome core particle and histone N-terminal tail modifications in the assembly and enzymatic activities of Reptin/Pontin. We demonstrate that purified Reptin and Pontin form stable complexes with nucleosomes. The ATPase activity of Reptin/Pontin is modulated by acetylation and methylation of the histone H3 N terminus. In vivo, association of Reptin with the progesterone receptor gene promoter is concomitant with changes in H3 marks of the surrounding nucleosomes. Furthermore, the presence of H3 tail peptides regulates the monomer-oligomer transition of Reptin/Pontin. Proteins that are pulled down by monomeric Reptin/Pontin differ from those that can bind to hexamers. We propose that changes in the oligomeric status of Reptin/Pontin create a platform that brings specific cofactors close to gene promoters and loads regulatory factors to establish an active state of chromatin.

KEYWORDS:

ATPase; Chromatin Remodeling; Histone Modification; Pontin/RUVBL1; Protein Conformation; Protein/DNA Interaction; Reptin/RUVBL2

PMID:
25336637
PMCID:
PMC4256336
DOI:
10.1074/jbc.M114.576785
[Indexed for MEDLINE]
Free PMC Article

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