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PLANT PHYSIOLOGY , Vol 115, Issue 1 93-100, Copyright © 1997 by American Society of Plant Biologists
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GENE REGULATION AND MOLECULAR GENETICS |
Phosphorylation by a Cyclin-Dependent Kinase Modulates DNA Binding of the Arabidopsis Heat-Shock Transcription Factor HSF1 in Vitro
A. Reindl, F. Schoffl, J. Schell, C. Koncz and L. Bako
Universitat Tubingen, Biologisches Institut, Lehrstuhl fur Allgemeine Genetik, Auf der Morgenstelle 28, D-72076 Tubingen, Germany (A.R., F.S.)
Phosphorylation is one of the mechanisms controlling the activity of
heat-shock transcription factors in yeast and mammalian cells. Here we
describe partial purification, identification, and characterization of a
protein kinase that phosphorylates the Arabidopsis heat-shock factor AtHSF1
at multiple serine residues. The HSF1 kinase forms a stable complex with
AtHSF1, which can be detected by kinase pull-down assays using a
histidine-tagged AtHSF1 substrate. The HSF1 kinase interacts with the
cell-cycle control protein Suc1p and is immunoprecipitated by an antibody
specific for the Arabidopsis cyclin-dependent CDC2a kinase. Phosphorylation
by CDC2a in vitro inhibits DNA binding of AtHSF1 to the cognate heat-shock
elements, suggesting a possible regulatory interaction between heat-shock
response and cell-cycle control in plants.
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