Truncation of αB-crystallin by the myopathy-causing Q151X mutation significantly destabilizes the protein leading to aggregate formation in transfected cells
VH Hayes, G Devlin, RA Quinlan - Journal of biological chemistry, 2008 - ASBMB
Here we investigate the effects of a myopathy-causing mutation in αB-crystallin, Q151X,
upon its structure and function. This mutation removes the C-terminal domain of αB-
crystallin, which is expected to compromise both its oligomerization and chaperone activity.
We compared this to two other αB-crystallin mutants (450delA, 464delCT) and also to a
series of C-terminal truncations (E164X, E165X, K174X, and A171X). We find that the effects
of the Q151X mutation were not always as predicted. Specifically, we have found that …
upon its structure and function. This mutation removes the C-terminal domain of αB-
crystallin, which is expected to compromise both its oligomerization and chaperone activity.
We compared this to two other αB-crystallin mutants (450delA, 464delCT) and also to a
series of C-terminal truncations (E164X, E165X, K174X, and A171X). We find that the effects
of the Q151X mutation were not always as predicted. Specifically, we have found that …
