Phosphorylation of Drosophila heat shock transcription factor

M. Fritsch, Carl Wu*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

14 Scopus citations


The role that phosphorylation plays in regulating heat shock factor (HSF) function and activity has been the subject of several studies. Here, we demonstrate that Drosophila melanogaster HSF (DmHSF) is a phosphoprotein that is multiply phosphorylated at some sites and is dephosphorylated at others upon heat shock. However, the steady-state level of phosphorylation of Drosophila HSF remains unchanged after heat shock. Phosphoamino-acid analysis reveals that predominantly serine residues are phosphorylated for both the non-shocked and heat shocked molecules. Gel mobility shift assays using extracts from SL2 cells treated with a variety of phosphatase and kinase inhibitors show little or no effect on the heat shock induced DNA binding activity of HSF or on its recovery. We conclude that phosphorylation plays no significant role in regulating the heat induced DNA binding activity of Drosophila HSF.

Original languageEnglish (US)
Pages (from-to)102-117
Number of pages16
JournalCell Stress and Chaperones
Issue number2
StatePublished - Jun 1999

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology

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