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Vol. 273, Issue 1, 286-290, January 2, 1998
From the Center for Ophthalmic Research, Brigham and Women's
Hospital, and Department of Ophthalmology, Harvard Medical School,
Boston, Massachusetts 02115
Lens
Intermolecular Exchange and Stabilization of Recombinant Human
A- and B-Crystallin
-crystallin subunits A and B are
differentially expressed and have a 3-to-1 ratio in most mammalian
lenses by intermolecular exchange. The biological significance of this
composition and the mechanism of exchange are not clear. Preparations
of human recombinant A- and B-crystallins provide a good system
in which to study this phenomenon. Both recombinant A- and
B-crystallins are folded and aggregated to the size of the native
-crystallin. During incubation together, they undergo an
intermolecular exchange as shown by native isoelectric focusing.
Circular dichroism measurements indicate that the protein with a 3-to-1
ratio of A- and B-crystallins has the same secondary structure
but somewhat different tertiary structures after exchange: the near-UV
CD increases after exchange. The resulting hybrid aggregate is more
stable than the individual homogeneous aggregates: at 62 °C,
B-crystallin is more susceptible to aggregation and displays a
greater light scattering than A-crystallin. This heat-induced
aggregation of B-crystallin, however, was suppressed by
intermolecular exchange with A-crystallin. These phenomena are also
observed by fast performance liquid chromatography gel filtration
patterns. The protein structure of B-crystallin is stabilized by
intermolecular exchange with A-crystallin.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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