Disulfide cross-links in the interaction of a cataract-linked alphaA-crystallin mutant with betaB1-crystallin.
FEBS Lett
; 583(1): 175-9, 2009 Jan 05.
Article
en En
| MEDLINE
| ID: mdl-19071118
ABSTRACT
A number of alphaA-crystallin mutants are associated with hereditary cataract including cysteine substitution at arginine 49. We report the formation of affinity-driven disulfide bonds in the interaction of alphaA-R49C with betaB1-crystallin. To mimic cysteine thiolation in the lens, betaB1-crystallin was modified by a bimane probe through a disulfide linkage. Our data suggest a mechanism whereby a transient disulfide bond occurs between alphaA- and betaB1-crystallin followed by a disulfide exchange with cysteine 49 of a neighboring alphaA-crystallin subunit. This is the first investigation of disulfide bonds in the confine of the chaperone/substrate complex where reaction rates are favored by orders of magnitude. Covalent protein cross-links are a hallmark of age-related cataract and may be a factor in its inherited form.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Catarata
/
Cisteína
/
Cadena A de alfa-Cristalina
/
Cadena B de beta-Cristalina
Límite:
Humans
Idioma:
En
Revista:
FEBS Lett
Año:
2009
Tipo del documento:
Article
País de afiliación:
Estados Unidos