Differential binding of mutant (R116C) and wildtype alphaA crystallin to actin.
OBJECTIVE
Quantitate the interaction of mutant (R116C) and wildtype human alphaA crystallins with actin.


METHODS
AlphaA crystallins, expressed in a recombinant system, were purified, followed by passage through an actin affinity column.


RESULTS
Binding of mutant alphaA crystallin was significantly less than binding of wildtype alphaA crystallin.


CONCLUSIONS
The R116C mutation of alphaA crystallin found in human cataracts binds less to the cytoskeletal component actin. Since both alphaA crystallin and actin are necessary for proper development of the lens, decreased binding of the mutant protein to actin may perturb normal differentiation processes of lens cells which are necessary for transparency.
Brown
Zachery
Z
Division of Biology, Kansas State University, Manhattan 97239, USA.
Ponce
Aldo
A
Lampi
Kirsten
K
Hancock
Lynn
L
Takemoto
Larry
L
D000199:Actins / Q000378:metabolism*; D002846:Chromatography, Affinity; D004926:Escherichia coli / Q000235:genetics; D015870:Gene Expression; D006801:Humans; D007223:Infant; D009154:Mutation; D011485:Protein Binding; D011994:Recombinant Proteins; D021241:Spectrometry, Mass, Electrospray Ionization; D038202:alpha-Crystallin A Chain / Q000235:genetics / Q000378:metabolism*
D000199:Actins; D011994:Recombinant Proteins; D038202:alpha-Crystallin A Chain