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Please use this identifier to cite or link to this item: http://idr.iitbbs.ac.in/jspui/handle/2008/237
Title: Acetylation of ?A-crystallin in the human lens: Effects on structure and chaperone function
Authors: Nagaraj R.H.
Nahomi R.B.
Shanthakumar S.
Linetsky M.
Padmanabha S.
Pasupuleti N.
Wang B.
Santhoshkumar P.
Panda A.K.
Biswas A.
Keywords: ?-Crystallin
Acetylation
Aging
Chaperone
Human lens
Lysine
Issue Date: 2012
Citation: 38
Abstract: ?-Crystallin is a major protein in the human lens that is perceived to help to maintain the transparency of the lens through its chaperone function. In this study, we demonstrate that many lens proteins including ?A-crystallin are acetylated in vivo. We found that K70 and K99 in ?A-crystallin and, K92 and K166 in ?B-crystallin are acetylated in the human lens. To determine the effect of acetylation on the chaperone function and structural changes, ?A-crystallin was acetylated using acetic anhydride. The resulting protein showed strong immunoreactivity against a N ?-acetyllysine antibody, which was directly related to the degree of acetylation. When compared to the unmodified protein, the chaperone function of the in vitro acetylated ?A-crystallin was higher against three of the four different client proteins tested. Because a lysine (residue 70; K70) in ?A-crystallin is acetylated in vivo, we generated a protein with an acetylation mimic, replacing Lys70 with glutamine (K70Q). The K70Q mutant protein showed increased chaperone function against three client proteins compared to the Wt protein but decreased chaperone function against ?-crystallin. The acetylated protein displayed higher surface hydrophobicity and tryptophan fluorescence, had altered secondary and tertiary structures and displayed decreased thermodynamic stability. Together, our data suggest that acetylation of ?A-crystallin occurs in the human lens and that it affects the chaperone function of the protein. � 2011 Elsevier B.V.
URI: http://dx.doi.org/10.1016/j.bbadis.2011.11.011
http://10.10.32.48:8080/jspui/handle/2008/237
Appears in Collections:Research Publications

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