TAF1 Activates Transcription by Phosphorylation of Serine 33 in Histone H2B

Maile, Tobias M.; Kwoczynski, Simona; Katzenberger, Rebeccah J.; Wassarman, David A.; Sauer, Frank

doi:10.1126/science.1095001

Cited by 62 publications

(42 citation statements)

References 25 publications

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“…There now are many known proteins in which O-GlcNAc and phosphate compete reciprocally for the same site on proteins (3). Here, all three sites also are known phosphorylation sites, although functional significance for phosphorylation has been identified only for Ser36 of H2B (Ser33 of H2B in Drosophila) (38)(39)(40)(41). H2B is phosphorylated at this site by TATA box binding protein (TBP) associated factor 1 (TAF1).…”

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

β- N -acetylglucosamine (O-GlcNAc) is part of the histone code

Sakabe

Wang

Hart

2010

Proc. Natl. Acad. Sci. U.S.A.

319

274

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Dynamic posttranslational modification of serine and threonine residues of nucleocytoplasmic proteins by β-N-acetylglucosamine (O-GlcNAc) is a regulator of cellular processes such as transcription, signaling, and protein-protein interactions. Like phosphorylation, O-GlcNAc cycles in response to a wide variety of stimuli. Although cycling of O-GlcNAc is catalyzed by only two highly conserved enzymes, O-GlcNAc transferase (OGT), which adds the sugar, and β-N-acetylglucosaminidase (O-GlcNAcase), which hydrolyzes it, the targeting of these enzymes is highly specific and is controlled by myriad interacting subunits. Here, we demonstrate by multiple specific immunological and enzymatic approaches that histones, the proteins that package DNA within the nucleus, are O-GlcNAcylated in vivo. Histones also are substrates for OGT in vitro. We identify O-GlcNAc sites on histones H2A, H2B, and H4 using mass spectrometry. Finally, we show that histone O-GlcNAcylation changes during mitosis and with heat shock. Taken together, these data show that O-GlcNAc cycles dynamically on histones and can be considered part of the histone code.epigenetics | histones

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Section: Resultsmentioning

confidence: 99%

“…H2B is phosphorylated at this site by TATA box binding protein (TBP) associated factor 1 (TAF1). Phosphorylated H2B is found in promoters of some genes that regulate the G2 to M-phase transition, suggesting that H2B phosphorylation could regulate cell-cycle progression (39).…”

Section: Resultsmentioning

confidence: 99%

β- N -acetylglucosamine (O-GlcNAc) is part of the histone code

Sakabe

Wang

Hart

2010

Proc. Natl. Acad. Sci. U.S.A.

319

274

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“…TAF1 bands were aligned based on other experiments in which S2 cell extracts were analyzed alongside ovary, testis, or head extracts. The asterisk indicates a potential cross-reacting band that was not observed with anti-TAF1-C antibody, which was raised against a polypeptide encoded by exons 12 to 14 of TAF1-4 (data not shown) (30). (B) Western blot analysis of S2 cell nuclear extracts for coimmunoprecipitation of TBP with TAF1-4.…”

Section: Reverse Transcriptase Pcr (Rt-pcr)mentioning

confidence: 99%

“…In flies, TAF1 null mutations are recessively lethal, and clonal analysis indicates that TAF1 is essential for cell proliferation or viability (55). Knockdown of TAF1 in D. melanogaster embryonic Schneider cell line 2 (S2) tissue culture cells by RNA interference (RNAi) results in cell cycle arrest in the G 2 /M phase (30). Thus, normal cell physiology is critically dependent on TAF1.…”

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confidence: 99%

ATM and ATR Pathways Signal Alternative Splicing of Drosophila TAF1 Pre-mRNA in Response to DNA Damage

Katzenberger

Marengo

Wassarman

2006

Molecular and Cellular Biology

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Alternative pre-mRNA splicing is a major mechanism utilized by eukaryotic organisms to expand their protein-coding capacity. To examine the role of cell signaling in regulating alternative splicing, we analyzed the splicing of the Drosophila melanogaster TAF1 pre-mRNA. TAF1 encodes a subunit of TFIID, which is broadly required for RNA polymerase II transcription. We demonstrate that TAF1 alternative splicing generates four mRNAs, TAF1-1, TAF1-2, TAF1-3, and TAF1-4, of which TAF1-2 and TAF1-4 encode proteins that directly bind DNA through AT hooks. TAF1 alternative splicing was regulated in a tissue-specific manner and in response to DNA damage induced by ionizing radiation or camptothecin. Pharmacological inhibitors and RNA interference were used to demonstrate that ionizing-radiation-induced upregulation of TAF1-3 and TAF1-4 splicing in S2 cells was mediated by the ATM (ataxia-telangiectasia mutated) DNA damage response kinase and checkpoint kinase 2 (CHK2), a known ATM substrate. Similarly, camptothecin-induced upregulation of TAF1-3 and TAF1-4 splicing was mediated by ATR (ATM-RAD3 related) and CHK1. These findings suggest that inducible TAF1 alternative splicing is a mechanism to regulate transcription in response to developmental or DNA damage signals and provide the first evidence that the ATM/CHK2 and ATR/CHK1 signaling pathways control gene expression by regulating alternative splicing.Alternative splicing is a major mechanism utilized by higher eukaryotic organisms to regulate gene expression during development and in response to stress (8,44,48,50). In fact, 35 to 74% of human genes may encode pre-mRNAs that are alternatively spliced (10,22,23,29,34). Alternative splicing can regulate whether or not a protein is produced, or it can generate pre-mRNAs that encode proteins with distinct functions (7,17). By analogy to other gene expression-regulatory mechanisms, such as transcription, it is probable that signal transduction pathways play a widespread role in controlling alternative splicing. However, documented examples of this phenomenon are limited, and a complete pathway has not been described.One of the most thoroughly understood examples of signaldependent alternative splicing is Ras signal-induced splicing of the CD44 pre-mRNA in humans (28,32,57). The Ras GTPase and the downstream mitogen-activated protein kinase (MAPK) signaling cascade specify inclusion of exon 5 (v5) in the mature CD44 mRNA. Stimuli that activate Ras lead to activation of MAPK, which in turn phosphorylates SAM68, an RNA-binding protein that interacts with an exonic splicing silencer element within v5. Phosphorylated SAM68 is then thought to interfere with the repressive activity of hnRNP A1 and allow factors bound to a v5 exonic splicing enhancer element to enhance v5 inclusion. Signal-dependent alternative splicing has also been implicated in the regulation of cellular processes, including apoptosis and the cell cycle (44, 47, 49). For instance, many genes encoding apoptotic regulators are alternatively spliced; however, littl...

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“…Lysyl-tRNA synthetase, with lysine-tRNA ligase activity, is a protein for transcription and tRNA processing and binds ATP, DNA and tRNA [36,37]. TBP associated factor 1 is involved in initiation of transcription and has been shown to bind ATP, DNA and proteins [38][39][40]. Zinc finger protein 333 is a transcription factor, participating in DNA binding and zinc binding [41,42].…”

Section: Protein Functional Classificationmentioning

confidence: 99%

Brain proteins interacting with the tetramerization region of non-erythroid alpha spectrin

Fung

2007

Cellular and Molecular Biology Letters

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Abstract:The N-terminal region of non-erythroid alpha spectrin (SpαII) is responsible for interacting with its binding partner, beta spectrin, to form functional spectrin tetramers. We used a yeast-two-hybrid system, with an N-terminal segment of alpha spectrin representing the functional tetramerization site, as a bait to screen human brain c-DNA library for proteins that interact with the alpha spectrin segment. In addition to several beta spectrin isoforms, we identified 14 proteins that interact with SpαII. Seven of the 14 were matched to 6 known proteins: Duo protein, Lysyl-tRNA synthetase, TBP associated factor 1, two isoforms (b and c) of a protein kinase A interacting protein and Zinc finger protein 333 (2 different segments). Four of the 6 proteins are located primarily in the nucleus, suggesting that spectrin plays important roles in nuclear functions. The remaining 7 proteins were unknown to the protein data base. Structural predictions show that many of the 14 proteins consist of a large portion of unstructured regions, suggesting that many of these proteins fold into a rather flexible conformation. It is interesting to note that all but 3 of the 14 proteins are predicted to consist of one to four coiled coils (amphiphilic helices). A mutation in SpαII, V22D, which interferes with the coiled coil bundling of SpαII with beta spectrin, also affects SpαII interaction with Duo protein, TBP associated factor 1 and Lysyl-tRNA synthetase, suggesting that they may compete with beta spectrin for interaction with SpαII. Future structural and functional studies of these proteins to provide interaction mechanisms will no doubt lead to a better understanding of brain physiology and pathophysiology.

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TAF1 Activates Transcription by Phosphorylation of Serine 33 in Histone H2B

Cited by 62 publications

References 25 publications

β- N -acetylglucosamine (O-GlcNAc) is part of the histone code

β- N -acetylglucosamine (O-GlcNAc) is part of the histone code

ATM and ATR Pathways Signal Alternative Splicing of Drosophila TAF1 Pre-mRNA in Response to DNA Damage

Brain proteins interacting with the tetramerization region of non-erythroid alpha spectrin

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