scholarly journals Histone Deacetylase 1 Is Essential for Rod Photoreceptor Differentiation by Regulating Acetylation at Histone H3 Lysine 9 and Histone H4 Lysine 12 in the Mouse Retina

2016 ◽  
Vol 292 (6) ◽  
pp. 2422-2440 ◽  
Author(s):  
Renata C. Ferreira ◽  
Evgenya Y. Popova ◽  
Jessica James ◽  
Marcelo R. S. Briones ◽  
Samuel S. Zhang ◽  
...  
Apmis ◽  
2008 ◽  
Vol 116 (5) ◽  
pp. 420-421
Author(s):  
Lena Marquard ◽  
Christian Bjørn Poulsen ◽  
Ib Jarle Christensen ◽  
Peter Buhl Ralfkiær ◽  
Maxwell Sehested

2009 ◽  
Vol 54 (6) ◽  
pp. 688-698 ◽  
Author(s):  
Lena Marquard ◽  
Christian B Poulsen ◽  
Lise Mette Gjerdrum ◽  
Peter de Nully Brown ◽  
Ib J Christensen ◽  
...  

2002 ◽  
Vol 22 (22) ◽  
pp. 7820-7830 ◽  
Author(s):  
Christoph Hauser ◽  
Bernd Schuettengruber ◽  
Stefan Bartl ◽  
Gerda Lagger ◽  
Christian Seiser

ABSTRACT Histone deacetylase 1 (HDAC1) is a major regulator of chromatin structure and gene expression. Tight control of HDAC1 expression is essential for normal cell cycle progression of mammalian cells. HDAC1 mRNA levels are regulated by growth factors and by changes in intracellular deacetylase activity levels. Stimulation of the mitogen-activated protein kinase cascade by anisomycin or growth factors, together with inhibition of deacetylases by trichostatin A (TSA), leads to stable histone H3 phosphoacetylation and strongly induced HDAC1 expression. In contrast, activation of the nucleosomal response by anisomycin alone results only in transient phosphoacetylation of histone H3 without affecting HDAC1 mRNA levels. The transcriptional induction of the HDAC1 gene by anisomycin and TSA is efficiently blocked by H89, an inhibitor of the nucleosomal response. Detailed studies of the kinetics of histone acetylation and phosphorylation show that the two modifications are synergistic and essential for induced HDAC1 transcription. Activation of the HDAC1 gene by anisomycin together with TSA or by growth factors is accompanied by phosphoacetylation of HDAC1 promoter-associated histone H3. Our results present evidence for a precise regulatory mechanism which allows induction of the HDAC1 gene in response to proliferation signals and modulation of HDAC1 expression dependent on intracellular deacetylase levels.


2005 ◽  
Vol 25 (23) ◽  
pp. 10338-10351 ◽  
Author(s):  
Zhijun Duan ◽  
Adrian Zarebski ◽  
Diego Montoya-Durango ◽  
H. Leighton Grimes ◽  
Marshall Horwitz

ABSTRACT The growth factor independent 1 (Gfi1) transcriptional regulator oncoprotein plays a crucial role in hematopoietic, inner ear, and pulmonary neuroendocrine cell development and governs cell processes as diverse as self-renewal of hematopoietic stem cells, proliferation, apoptosis, differentiation, cell fate specification, and oncogenesis. However, the molecular basis of its transcriptional functions has remained elusive. Here we show that Gfi1 recruits the histone lysine methyltransferase G9a and the histone deacetylase 1 (HDAC1) in order to modify the chromatin of genes targeted for repression by Gfi1. G9a and HDAC1 are both in a repressive complex assembled by Gfi1. Endogenous Gfi1 colocalizes with G9a, HDAC1, and K9-dimethylated histone H3. Gfi1 associates with G9a and HDAC1 on the promoter of the cell cycle regulator p21 Cip/WAF1 , resulting in an increase in K9 dimethylation at histone H3. Silencing of Gfi1 expression in myeloid cells reverses G9a and HDAC1 recruitment to p21 Cip/WAF1 and elevates its expression. These findings highlight the role of epigenetics in the regulation of development and oncogenesis by Gfi1.


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