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TAF1 Activates Transcription by Phosphorylation of Serine 33 in Histone H2B
Rebeccah J. Katzenberger,3
David A. Wassarman,3
Dynamic changes in chromatin structure, induced by posttranslationalmodification of histones, play a fundamental role in regulatingeukaryotic transcription. Here we report that histone H2B isphosphorylated at evolutionarily conserved Ser33 (H2B-S33) bythe carboxyl-terminal kinase domain (CTK) of the DrosophilaTFIID subunit TAF1. Phosphorylation of H2B-S33 at the promoterof the cell cycle regulatory gene string and the segmentationgene giant coincides with transcriptional activation. Eliminationof TAF1 CTK activity in Drosophila cells and embryos reducestranscriptional activation and phosphorylation of H2B-S33. Thesedata reveal that H2B-S33 is a physiological substrate for theTAF1 CTK and that H2B-S33 phosphorylation is essential for transcriptionalactivation events that promote cell cycle progression and development.
1 Department of Biochemistry, University of CaliforniaRiverside, Riverside, CA 95121, USA. 2 Zentrum für Molekulare Biologie der Universität Heidelberg (ZMBH), Im Neuenheimer Feld 282, 69120 Heidelberg, Germany. 3 Department of Pharmacology, University of Wisconsin (UW)Madison, 1300 University Avenue, Madison, WI 53706, USA.