| First Author | Kumar MS | Year | 2009 |
| Journal | FEBS Lett | Volume | 583 |
| Issue | 1 | Pages | 175-9 |
| PubMed ID | 19071118 | Mgi Jnum | J:201311 |
| Mgi Id | MGI:5512956 | Doi | 10.1016/j.febslet.2008.11.047 |
| Citation | Kumar MS, et al. (2009) Disulfide cross-links in the interaction of a cataract-linked alphaA-crystallin mutant with betaB1-crystallin. FEBS Lett 583(1):175-9 |
| abstractText | 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. |
