 The
family of heat shock proteins was initially
characterized as a highly conserved battery of
genes whose expression could be induced by heat
shock. Many heat shock protein family members
are now known to function constitutively as
molecular chaperones, stabilizing and assisting
in the trafficking of nascent peptides during
normal growth. Under stressful conditions such
as heat shock or hypoxia, increased expression
of heat shock proteins protects the cell by
stabilizing unfolded or misfolded peptides,
giving the cell time to repair or re-synthesize
damaged proteins.
Many heat shock proteins function together in co-chaperone
complexes, such as
Hsp70/Hsp40
(bacterial
DnaK/DnaJ)
that along with
GrpE acts as an ATP-regulated shuttle
complex for newly synthesized proteins. Many of
these nascent peptides are delivered to
Hsp90-containing complexes, which play a
critical role in the stabilization and
activation of key signaling kinases and hormone
receptors. The
Hsp60/Hsp10
complex (bacterial
GroEL/GroES)
forms an alternative protein folding mechanism
in the mitochondria. Small heat shock proteins
including
Hsp27 and the
crystallins form large oligomeric complexes
that function to prevent protein aggregation.
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+32
1658 9045
+32
1650 9045
