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XB-ART-45342
Nucleus. November 1, 2011; 2 (6): 580-90.

Barrier-to-Autointegration Factor influences specific histone modifications.

Montes de Oca R , Andreassen PR , Wilson KL .


Abstract
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
PMC ID: PMC3324346
Article link: Nucleus.
Grant support: R01 GM48646 NIGMS NIH HHS

Genes referenced: banf1 celsr1 hdac1 krt14 me1 me3 ppp2r4 psmd6 set
Antibodies referenced:
Morpholinos referenced:

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