Does post-translational modification influence chaperone-like activity of alpha-crystallin? I. Study on phosphorylation.
It is difficult to isolate derivatives of alpha-crystallin with only one type of post-translational modification, because this protein is subjected to several different types of modification. In the present study using bovine lens proteins, we isolated mono-phosphorylated alphaB-crystallin with no other post-translational modifications. Using this material, we demonstrated that mono-phosphorylation reduced the activity of alphaB-crystallin by approximately 30%. Our results confirmed that investigation of the correlation between chaperone-like activities of alpha-crystallin and post-translational modification is important to understand the mechanism of cataract formation.
Kamei
A
A
Department of Biochemistry, Faculty of Pharmaceutical Sciences, Meijo University, Aichi, Japan. kamei@meijo-u.ac.jp
Hamaguchi
T
T
Matsuura
N
N
Masuda
K
K
D000818:Animals; D002417:Cattle; D018833:Chaperonins / Q000378:metabolism*; D003459:Crystallins / Q000378:metabolism*; D013058:Mass Spectrometry / Q000379:methods; D010766:Phosphorylation; D011499:Protein Processing, Post-Translational
D003459:Crystallins; D018833:Chaperonins