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J. Biol. Chem., Vol. 275, Issue 29, 22009-22013, July 21, 2000
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A and B Crystallins Affects
Oligomerization and Enhances Chaperone-like Activity*
and
From the Centre for Cellular and Molecular Biology,
Hyderabad 500007, India
A and B crystallins, members of the small
heat shock protein family, prevent aggregation of proteins by their
chaperone-like activity. These two proteins, although very homologous,
particularly in the C-terminal region, which contains the highly
conserved "-crystallin domain," show differences in their
protective ability toward aggregation-prone target proteins. In order
to investigate the differences between A and B crystallins, we
engineered two chimeric proteins, ANBC and BNAC, by swapping the
N-terminal domains of A and B crystallins. The chimeras were
cloned and expressed in Escherichia coli. The purified
recombinant wild-type and chimeric proteins were characterized by
fluorescence and circular dichroism spectroscopy and gel permeation
chromatography to study the changes in secondary, tertiary, and
quaternary structure. Circular dichroism studies show structural
changes in the chimeric proteins. BNAC binds more
8-anilinonaphthalene-1-sulfonic acid than the ANBC and the wild-type
proteins, indicating increased accessible hydrophobic regions. The
oligomeric state of ANBC is comparable to wild-type B
homoaggregate. However, there is a large increase in the oligomer size
of the BNAC chimera. Interestingly, swapping domains results in
complete loss of chaperone-like activity of ANBC, whereas BNAC
shows severalfold increase in its protective ability. Our findings show
the importance of the N- and C-terminal domains of A and B
crystallins in subunit oligomerization and chaperone-like activity.
Domain swapping results in an engineered protein with significantly
enhanced chaperone-like activity.
Recipient of a senior research fellowship from the University
Grants Commission, Government of India.
§
To whom correspondence should be addressed. Tel.: 91-40-717-2241;
Fax: 91-40-717-1195; E-mail: mohan@ccmb.ap.nic.in.
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