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- W2981554920 endingPage "4518" @default.
- W2981554920 startingPage "4505" @default.
- W2981554920 abstract "The βγ-crystallin superfamily contains both β- and γ-crystallins of the vertebrate eye lens and the microbial calcium-binding proteins, all of which are characterized by a common double-Greek key domain structure. The vertebrate βγ-crystallins are long-lived structural proteins that refract light onto the retina. In contrast, the microbial βγ-crystallins bind calcium ions. The βγ-crystallin from the tunicate Ciona intestinalis (Ci-βγ) provides a potential link between these two functions. It binds calcium with high affinity and is found in a light-sensitive sensory organ that is highly enriched in metal ions. Thus, Ci-βγ is valuable for investigating the evolution of the βγ-crystallin fold away from calcium binding and toward stability in the apo form as part of the vertebrate lens. Here, we investigate the effect of Ca2+ and other divalent cations on the stability and aggregation propensity of Ci-βγ and human γS-crystallin (HγS). Beyond Ca2+, Ci-βγ is capable of coordinating Mg2+, Sr2+, Co2+, Mn2+, Ni2+, and Zn2+, although only Sr2+ is bound with comparable affinity to its preferred metal ion. The extent to which the tested divalent cations stabilize Ci-βγ structure correlates strongly with ionic radius. In contrast, none of the tested divalent cations improved the stability of HγS, and some of them induced aggregation. Zn2+, Ni2+, and Co2+ induce aggregation by interacting with cysteine residues, whereas Cu2+-mediated aggregation proceeds via a different binding site." @default.
- W2981554920 created "2019-11-01" @default.
- W2981554920 creator A5007750506 @default.
- W2981554920 creator A5014591864 @default.
- W2981554920 creator A5034330702 @default.
- W2981554920 creator A5043999172 @default.
- W2981554920 creator A5049169994 @default.
- W2981554920 date "2019-10-24" @default.
- W2981554920 modified "2023-10-18" @default.
- W2981554920 title "Divalent Cations and the Divergence of <i>βγ</i>-Crystallin Function" @default.
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