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Barrier-to-Autointegration Factor influences specific histone modifications.

Defects in the nuclear envelope or nuclear 'lamina' networks cause disease and can perturb histone posttranslational (epigenetic) regulation. Barrier-to-Autointegration Factor (BAF) is an essential but enigmatic lamina component that binds lamins, LEM-domain proteins, DNA and histone H3 directly. We report that BAF copurified with nuclease-digested mononucleosomes and associated with modified histones in vivo. BAF overexpression significantly reduced global histone H3 acetylation by 18%. In cells that stably overexpressed BAF 3-fold, silencing mark H3-K27-Me1/3 and active marks H4-K16-Ac and H4-Ac5 decreased significantly. Significant increases were also seen for silencing mark H3-K9-Me3, active marks H3-K4-Me2, H3-K9/K14-Ac and H4-K5-Ac and a mark (H3-K79-Me2) associated with both active and silent chromatin. Other increases (H3-S10-P, H3-S28-P and silencing mark H3-K9-Me2) did not reach statistical significance. BAF overexpression also significantly influenced cell cycle distribution. Moreover, BAF associated in vivo with SET/I2PP2A (protein phosphatase 2A inhibitor; blocks H3 dephosphorylation) and G9a (H3-K9 methyltransferase), but showed no detectable association with HDAC1 or HATs. These findings reveal BAF as a novel epigenetic regulator and are discussed in relation to BAF deficiency phenotypes, which include a hereditary progeria syndrome and loss of pluripotency in embryonic stem cells.

Pubmed ID: 22127260


  • Montes de Oca R
  • Andreassen PR
  • Wilson KL


Nucleus (Austin, Tex.)

Publication Data

February 9, 2012

Associated Grants

  • Agency: NIGMS NIH HHS, Id: R01 GM48646

Mesh Terms

  • Acetylation
  • Animals
  • Cell Cycle
  • DNA-Binding Proteins
  • Epigenesis, Genetic
  • HeLa Cells
  • Histone Chaperones
  • Histone Deacetylase 1
  • Histones
  • Humans
  • Lamins
  • Nuclear Lamina
  • Nuclear Proteins
  • Progeria
  • Protein Processing, Post-Translational
  • Transcription Factors
  • Xenopus laevis