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J Biol Chem, Vol. 274, Issue 14, 9378-9385, April 2, 1999
From the Centre de recherche en cancérologie de
l'Université Laval, L'Hôtel-Dieu de Québec,
Québec, Québec G1R 2J6, Canada
Distinct biochemical activities have been
reported for small and large molecular complexes of heat shock protein
27 (HSP27), respectively. Using glycerol gradient ultracentrifugation
and chemical cross-linking, we show here that Chinese hamster HSP27 is
expressed in cells as homotypic multimers ranging from dimers up to
700-kDa oligomers. Treatments with arsenite, which induces phosphorylation on Ser15 and Ser90,
provoked a major change in the size distribution of the complexes that
shifted from oligomers to dimers. Ser90 phosphorylation was
sufficient and necessary for causing this change in structure. Dimer
formation was severely inhibited by replacing Ser90 with
Ala90 but not by replacing Ser15 with
Ala15. Using the yeast two-hybrid system, two domains were
identified that were responsible for HSP27 intermolecular interactions.
One domain was insensitive to phosphorylation and corresponded to the
C-terminal 
-crystallin domain. The other domain was sensitive to
serine 90 phosphorylation and was located in the N-terminal region of
the protein. Fusion of this N-terminal domain to firefly luciferase
conferred luciferase with the capacity to form multimers that
dissociated into monomers upon phosphorylation. A deletion within this
domain of residues Arg5-Tyr23, which contains
a WDPF motif found in most proteins of the small heat shock protein
family, yielded a protein that forms only phosphorylation-insensitive dimers. We propose that HSP27 forms stable dimers through the -crystallin domain. These dimers further multimerize through intermolecular interactions mediated by the phosphorylation-sensitive N-terminal domain.
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