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Science 14 May 2004:
Vol. 304. no. 5673, pp. 1010 - 1014
DOI: 10.1126/science.1095001
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Reports

TAF1 Activates Transcription by Phosphorylation of Serine 33 in Histone H2B

Tobias Maile,1* Simona Kwoczynski,2*{dagger} Rebeccah J. Katzenberger,3 David A. Wassarman,3{ddagger} Frank Sauer1,2{ddagger}

Dynamic changes in chromatin structure, induced by posttranslational modification of histones, play a fundamental role in regulating eukaryotic transcription. Here we report that histone H2B is phosphorylated at evolutionarily conserved Ser33 (H2B-S33) by the carboxyl-terminal kinase domain (CTK) of the Drosophila TFIID subunit TAF1. Phosphorylation of H2B-S33 at the promoter of the cell cycle regulatory gene string and the segmentation gene giant coincides with transcriptional activation. Elimination of TAF1 CTK activity in Drosophila cells and embryos reduces transcriptional activation and phosphorylation of H2B-S33. These data reveal that H2B-S33 is a physiological substrate for the TAF1 CTK and that H2B-S33 phosphorylation is essential for transcriptional activation events that promote cell cycle progression and development.

1 Department of Biochemistry, University of California–Riverside, 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.


* These authors contributed equally to this work.

{dagger} Present address: Heidelberger Institut für Pflanzenwis-senschaften, Ruprecht-Karls-Universität Heidelberg, Im Neuenheimer Feld 230, 69120 Heidelberg, Germany.

{ddagger} To whom correspondence should be addressed. E-mail: frank.sauer{at}ucr.edu (F.S.), dawassarman{at}wisc.edu (D.A.W.)

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Science. ISSN 0036-8075 (print), 1095-9203 (online)