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J Biol Chem, Vol. 274, Issue 27, 18947-18956, July 2, 1999
by Phosphorylation
,
,,,
From the The small heat shock proteins (sHsps) from human
(Hsp27) and mouse (Hsp25) form large oligomers which can act as
molecular chaperones in vitro and protect cells from heat
shock and oxidative stress when overexpressed. In addition, mammalian
sHsps are rapidly phosphorylated by MAPKAP kinase 2/3 at two or three
serine residues in response to various extracellular stresses. Here we
analyze the effect of sHsp phosphorylation on its quaternary structure, chaperone function, and protection against oxidative stress. We show
that in vitro phosphorylation of recombinant sHsp as well as molecular mimicry of Hsp27 phosphorylation lead to a significant decrease of the oligomeric size. We demonstrate that both
phosphorylated sHsps and the triple mutant Hsp27-S15D,S78D,S82D show
significantly decreased abilities to act as molecular chaperones
suppressing thermal denaturation and facilitating refolding of citrate
synthase in vitro. In parallel, Hsp27 and its mutants
were analyzed for their ability to confer resistance against oxidative
stress when overexpressed in L929 and 13.S.1.24 cells. While wild type
Hsp27 confers resistance, the triple mutant S15D,S78D,S82D cannot
protect against oxidative stress effectively. These data indicate that large oligomers of sHsps are necessary for chaperone action and resistance against oxidative stress whereas phosphorylation
down-regulates these activities by dissociation of sHsp complexes to tetramers.
Max-Delbrück-Centrum für
Molecule Medizin, Robert-Rössle-Str. 10, D-13122 Berlin, Germany,
the § Institut für Biophysik und Physikalische
Biochemie, Universität Regensburg, D-93040 Regensburg, Germany,
the ¶ Laboratoire du Stress Cellulaire, Centre de
Génétique Moléculaire et Cellulaire, CNRS-UMR-5534,
Université Claude Bernard Lyon-I, F-69622 Villeurbanne, France,
and the Martin-Luther-Universität Halle-Wittenberg,
Innovationskolleg Zellspezialisierung, Hoher Weg 8, D-06120 Halle, Germany
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