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J Biol Chem, Vol. 274, Issue 47, 33235-33243, November 19, 1999
B-crystallin
Alters Its Protein Structure, Chaperone Activity, and Interaction
with Intermediate Filaments in Vitro
,,,
, and
From the Desmin-related myopathy and cataract are both
caused by the R120G mutation in Department of Biochemistry, Medical Science
Institute, The University, Dundee DD1 5EH, United Kingdom and the
Departments of ¶ Biological Structure and Ophthalmology,
University of Washington, Seattle, Washington 98195-7420
B-crystallin. Desmin-related
myopathy is one of several diseases characterized by the coaggregation
of intermediate filaments with B-crystallin, and it identifies
intermediate filaments as important physiological substrates for
B-crystallin. Using recombinant human B-crystallin, the effects
of the disease-causing mutation R120G upon the structure and the
chaperone activities of B-crystallin are reported. The secondary,
tertiary, and quaternary structural features of B-crystallin are all
altered by the mutation as deduced by near- and far-UV circular
dichroism spectroscopy, size exclusion chromatography, and chymotryptic
digestion assays. The R120G B-crystallin is also less stable than
wild type B-crystallin to heat-induced denaturation. These
structural changes coincide with a significant reduction in the
in vitro chaperone activity of the mutant B-crystallin
protein, as assessed by temperature-induced protein aggregation assays.
The mutation also significantly altered the interaction of
B-crystallin with intermediate filaments. It abolished the ability
of B-crystallin to prevent those filament-filament interactions
required to induce gel formation while increasing B-crystallin
binding to assembled intermediate filaments. These activities are
closely correlated to the observed disease pathologies characterized by
filament aggregation accompanied by B-crystallin binding. These
studies provide important insight into the mechanism of
B-crystallin-induced aggregation of intermediate filaments that
causes disease.
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