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Molecular and Cellular Biology, September 2003, p. 6129-6138, Vol. 23, No. 17
0270-7306/03/$08.00+0     DOI: 10.1128/MCB.23.17.6129-6138.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Protein Phosphatase 2A Activity Affects Histone H3 Phosphorylation and Transcription in Drosophila melanogaster

Scott J. Nowak, Chi-Yun Pai, and Victor G. Corces*

Department of Biology, The Johns Hopkins University, Baltimore, Maryland 21218

Received 19 March 2003/ Returned for modification 15 April 2003/ Accepted 6 June 2003

Transcriptional activation of the heat shock genes during the heat shock response in Drosophila has been intimately linked to phosphorylation of histone H3 at serine 10, whereas repression of non-heat-shock genes correlates with dephosphorylation of histone H3. It is then possible that specific kinase and/or phosphatase activities may regulate histone phosphorylation and therefore transcription activation and repression, respectively. We find that treatment of cells with strong phosphatase inhibitors interferes with the genome-wide dephosphorylation of histone H3 normally observed at non-heat-shock genes during heat shock. Mutants in protein phosphatase type 2A (PP2A) also display reduced genome-wide H3 dephosphorylation, and sites of H3 phosphorylation that do not contain heat shock genes remain transcriptionally active during heat shock in PP2A mutants. Finally, the SET protein, a potent and highly selective inhibitor of PP2A activity that inhibits PP2A-mediated dephosphorylation of Ser10-phosphorylated H3, is detected at transcriptionally active regions of polytene chromosomes. These results suggest that activation and repression of gene expression during heat shock might be regulated by changes in PP2A activity controlled by the SET protein.

* Corresponding author. Mailing address: Department of Biology, The Johns Hopkins University, 3400 N. Charles St., Baltimore, MD 21218. Phone: (410) 516-8749. Fax: (410) 516-5456. E-mail: corces{at}jhu.edu. {dagger} Present address: Skirball Institute of Biomolecular Medicine, New York, NY 10016.

Molecular and Cellular Biology, September 2003, p. 6129-6138, Vol. 23, No. 17
0022-538X/03/$08.00+0     DOI: 10.1128/MCB.23.17.6129-6138.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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