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J Biol Chem, Vol. 273, Issue 15, 8749-8755, April 10, 1998
From the Department of Biochemistry and Molecular Biology,
University of Miami School of Medicine, Miami, Florida 33136
Mapping of tryptic phosphopeptides of heat shock
factor 1 (HSF1) from non-stressed or moderately heat-stressed HeLa
cells, labeled in vivo by
[32P]orthophosphate, revealed four major phosphopeptides
A to D. Heat stress drastically increased phosphopeptide signals. To
identify target peptides and amino acids and to correlate
phosphorylation and transactivation function, phosphopeptide maps were
produced of LexA-human HSF1 chimeras and mutant derivatives thereof,
and transactivation activities of original and mutant chimeras were compared. LexA-HSF1 chimeras were previously shown to be regulated identically to HSF1, except that they transactivate promoters with
LexA-binding sites instead of hsp promoters. The patterns of
phosphopeptides of LexA-HSF1 and endogenous HSF1 were similar. Analysis
of single residue substitutions suggested that phosphopeptide C is
peptide VKEEPPSPPQSPR (297-309) phosphorylated on Ser-307 but not
Ser-303. Substitution of Ser-307 but not Ser-303 caused deregulation of
factor activity. Mapping of several constitutively active chimeras
associated unphosphorylated peptide C with the transcriptionally active
HSF1 conformation, suggesting that dephosphorylation of this peptide
(at Ser-307) may either be an integral step in the activation process
or serve to maintain the active conformation of HSF1. Exploiting this
correlation, indirect evidence was obtained that activation domains of
HSF1 interact with the distantly located regulatory domain to maintain
the factor in an inactive state.
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