ALPHA-CRYSTALLIN QUATERNARY STRUCTURE - MOLECULAR-BASIS FOR ITS CHAPERONE ACTIVITY

被引：27

作者：

SINGH, K

GROTHVASSELLI, B

KUMOSINSKI, TF

FARNSWORTH, PN

机构：

[1] UNIV MED & DENT NEW JERSEY,NEW JERSEY MED SCH,DEPT PHYSIOL,NEWARK,NJ 07103

[2] UNIV MED & DENT NEW JERSEY,NEW JERSEY MED SCH,DEPT OPHTHALMOL,NEWARK,NJ 07103

[3] USDA ARS,EASTERN REG RES CTR,DEPT MACROMOLEC,PHILADELPHIA,PA 19118

[4] USDA ARS,EASTERN REG RES CTR,DEPT CELL STRUCT,PHILADELPHIA,PA 19118

来源：

FEBS LETTERS | 1995年 / 372卷 / 2-3期

关键词：

ALPHA-CRYSTALLIN; CHAPERONE; GAMMA-CRYSTALLIN; LENS;

D O I：

10.1016/0014-5793(95)00980-N

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

alpha-Crystallin, the major protein in all vertebrate lenses, functions as a chaperone. In the present analysis, an 'open' micellar structure composed of alpha A subunits is used to simulate chaperoning of partially heat denatured soluble gamma-crystallin. The interaction is both electrostatic and hydrophobic and satisfies experimental evidence for a 1:1 alpha/gamma molar ratio, a doubling of molecular mass and a minimal increase in the dimensions of the complex [J. Biol. Chem. (1994) 269, 13601-13608; Invest. Opthalmol. Vis. Sci. (1995) 36, 311-21]. These data are also in accord with Farahbaksh et al. [Biochemistry (1995) 34, 509-16]; i.e. the bound gamma-crystallin monomers are not in a central cavity, but are separated by alpha A subunits.

引用

页码：283 / 287

页数：5

共 28 条

[1] A POSSIBLE STRUCTURE FOR ALPHA-CRYSTALLIN [J].