scholarly journals Acetylation of Histones and Transcription-Related Factors

2000 ◽  
Vol 64 (2) ◽  
pp. 435-459 ◽  
Author(s):  
David E. Sterner ◽  
Shelley L. Berger
Keyword(s):  
Histone Acetyltransferase ◽  
Binding Protein ◽  
Rna Polymerase Iii ◽  
High Mobility ◽  
General Factor ◽  
Creb Binding Protein ◽  
Related Factors ◽  
Nuclear Receptor Coactivators ◽  
Chromatin Proteins ◽  
Related Proteins

SUMMARY The state of chromatin (the packaging of DNA in eukaryotes) has long been recognized to have major effects on levels of gene expression, and numerous chromatin-altering strategies—including ATP-dependent remodeling and histone modification—are employed in the cell to bring about transcriptional regulation. Of these, histone acetylation is one of the best characterized, as recent years have seen the identification and further study of many histone acetyltransferase (HAT) proteins and their associated complexes. Interestingly, most of these proteins were previously shown to have coactivator or other transcription-related functions. Confirmed and putative HAT proteins have been identified from various organisms from yeast to humans, and they include Gcn5-related N-acetyltransferase (GNAT) superfamily members Gcn5, PCAF, Elp3, Hpa2, and Hat1: MYST proteins Sas2, Sas3, Esa1, MOF, Tip60, MOZ, MORF, and HBO1; global coactivators p300 and CREB-binding protein; nuclear receptor coactivators SRC-1, ACTR, and TIF2; TATA-binding protein-associated factor TAFII250 and its homologs; and subunits of RNA polymerase III general factor TFIIIC. The acetylation and transcriptional functions of these HATs and the native complexes containing them (such as yeast SAGA, NuA4, and possibly analogous human complexes) are discussed. In addition, some of these HATs are also known to modify certain nonhistone transcription-related proteins, including high-mobility-group chromatin proteins, activators such as p53, coactivators, and general factors. Thus, we also detail these known factor acetyltransferase (FAT) substrates and the demonstrated or potential roles of their acetylation in transcriptional processes.

Temporal/spatial expression of nuclear receptor coactivators in the mouse lung

2000 ◽  
Vol 279 (6) ◽  
pp. L1066-L1074 ◽  
Author(s):  
Angela Naltner ◽  
Susan Wert ◽  
Jeffrey A. Whitsett ◽  
Cong Yan
Keyword(s):  
Retinoic Acid ◽  
Epithelial Cells ◽  
Nuclear Receptor ◽  
Binding Protein ◽  
Mouse Lung ◽  
Alveolar Type ◽  
Type I ◽  
Type Ii ◽  
Creb Binding Protein ◽  
Nuclear Receptor Coactivators

Our laboratory has previously demonstrated that retinoic acid nuclear receptor, thyroid transcription factor-1 (TTF-1), and nuclear receptor coactivators such as cAMP response element binding protein (CREB) binding protein (CBP)/p300 and steroid receptor coactivator-1 (SRC-1) form an enhanceosome on the 5′-enhancer region of the human surfactant protein B gene. Immunohistochemistry was used to identify cells that coexpressed CBP/p300, SRC-1, retinoid X receptor, and TTF-1 in the developing and mature lung. CBP/p300 and SRC-1 were expressed in the adult mouse lung, CBP and p300 being present in both alveolar type I and type II epithelial cells and SRC-1 and TTF-1 being restricted to type II epithelial cells. CBP/p300, SRC-1, and TTF-1 were readily detected in the nuclei of developing respiratory epithelial tubules in fetal mice from embryonic days 10 to 18.CBP/p300 and SRC-1 were also detected in developing mesenchymal cells. These coactivators were coexpressed with TTF-1 and SP-B in human pulmonary adenocarcinoma cells (H441 cells) in vitro. Interaction assays with a two-hybrid reporter analysis demonstrated direct interactions among TTF-1, SRC-1, and CBP/p300 in H441 cells. These findings support a role for retinoic acid receptor and nuclear receptor coactivators in the regulation of SP-B gene expression in the respiratory epithelium.

scholarly journals Transcriptional Activation by NF-κB Requires Multiple Coactivators

1999 ◽  
Vol 19 (9) ◽  
pp. 6367-6378 ◽  
Author(s):  
Kelly-Ann Sheppard ◽  
David W. Rose ◽  
Zaffar K. Haque ◽  
Riki Kurokawa ◽  
Eileen McInerney ◽  
...  
Keyword(s):  
Gene Expression ◽  
Transcriptional Activation ◽  
Histone Acetyltransferase ◽  
Binding Protein ◽  
Nuclear Factor Κb ◽  
Nuclear Factor ◽  
Creb Binding Protein ◽  
Element Binding Protein ◽  
Cyclic Amp Response Element ◽  
Coactivator Complex

ABSTRACT Nuclear factor-κB (NF-κB) plays a role in the transcriptional regulation of genes involved in inflammation and cell survival. In this report we demonstrate that NF-κB recruits a coactivator complex that has striking similarities to that recruited by nuclear receptors. Inactivation of either cyclic AMP response element binding protein (CREB)-binding protein (CBP), members of the p160 family of coactivators, or the CBP-associated factor (p/CAF) by nuclear antibody microinjection prevents NF-κB-dependent transactivation. Like nuclear receptor-dependent gene expression, NF-κB-dependent gene expression requires specific LXXLL motifs in one of the p160 family members, and enhancement of NF-κB activity requires the histone acetyltransferase (HAT) activity of p/CAF but not that of CBP. This coactivator complex is differentially recruited by members of the Rel family. The p50 homodimer fails to recruit coactivators, although the p50-p65 heterodimeric form of the transcription factor assembles the integrator complex. These findings provide new mechanistic insights into how this family of dimeric transcription factors has a differential effect on gene expression.

scholarly journals Interplay Between BALL and CREB Binding Protein Maintains H3K27 Acetylation on Active Genes in Drosophila

2021 ◽  
Vol 9 ◽  
Author(s):  
Ammad Shaukat ◽  
Muhammad Haider Farooq Khan ◽  
Hina Ahmad ◽  
Zain Umer ◽  
Muhammad Tariq
Keyword(s):  
Histone Acetyltransferase ◽  
Binding Protein ◽  
Gene Activation ◽  
Creb Binding Protein ◽  
Drastic Reduction ◽  
Trithorax Group ◽  
Genome Wide ◽  
Histone Kinase ◽  
Trithorax Group Proteins ◽  
Active Genes

CREB binding protein (CBP) is a multifunctional transcriptional co-activator that interacts with a variety of transcription factors and acts as a histone acetyltransferase. In Drosophila, CBP mediated acetylation of histone H3 lysine 27 (H3K27ac) is a known hallmark of gene activation regulated by trithorax group proteins (trxG). Recently, we have shown that a histone kinase Ballchen (BALL) substantially co-localizes with H3K27ac at trxG target loci and is required to maintain gene activation in Drosophila. Here, we report a previously unknown interaction between BALL and CBP, which positively regulates H3K27ac. Analysis of genome-wide binding profile of BALL and CBP reveals major overlap and their co-localization at actively transcribed genes. We show that BALL biochemically interacts with CBP and depletion of BALL results in drastic reduction in H3K27ac. Together, these results demonstrate a previously unknown synergy between BALL and CBP and reveals a potentially new pathway required to maintain gene activation during development.

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