Abundant Perithecial Protein (APP) from Neurospora is a primitive functional analog of ocular crystallins

Pawar, Asmita D.; Kiran, Uday; Raman, Rajeev; Chandani, Sushil; Sharma, Yogendra

doi:10.1016/j.bbrc.2019.06.102

Cited by 1 publication

(2 citation statements)

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“…[6,20] This process is illustrated by the Neurospora crassa abundant perithecial protein (APP), an early crystallin orthologue that is highly aggregation-resistant at high protein concentrations and lacks functional calcium ion binding sites. [196] Unlike related proteins, human βγ-crystallins lack the ability to bind Ca 2 + . [197] Increased divalent cation concentration in the eye lens, which can be caused by aging, [162] smoking, [198,199] or diabetes, [200,201] is associated with lens opacification and cataract formation.…”

Section: Metal Ion-induced Interactionsmentioning

confidence: 99%

“…The pathway for crystallin evolution is generally assumed to be selection for stability and solubility, often followed by loss of the original activity, in this case metal binding, along the way to gaining its new optical function [6,20] . This process is illustrated by the Neurospora crassa abundant perithecial protein (APP), an early crystallin orthologue that is highly aggregation‐resistant at high protein concentrations and lacks functional calcium ion binding sites [196] . Unlike related proteins, human βγ‐crystallins lack the ability to bind Ca 2+ [197] …”

Section: Metal Ion‐induced Interactionsmentioning

confidence: 99%

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Chemical Properties Determine Solubility and Stability in βγ‐Crystallins of the Eye Lens

et al. 2021

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βγ-Crystallins are the primary structural and refractive proteins found in the vertebrate eye lens. Because crystallins are not replaced after early eye development, their solubility and stability must be maintained for a lifetime, which is even more remarkable given the high protein concentration in the lens. Aggregation of crystallins caused by mutations or post-translational modifications can reduce crystallin protein stability and alter intermolecular interactions. Common post-translational modifications that can cause age-related cataracts include deamidation, oxidation, and tryptophan derivatization. Metal ion binding can also trigger reduced crystallin solubility through a variety of mechanisms. Interprotein interactions are critical to maintaining lens transparency: crystallins can undergo domain swapping, disulfide bonding, and liquid-liquid phase separation, all of which can cause opacity depending on the context. Important experimental techniques for assessing crystallin conformation in the absence of a high-resolution structure include dye-binding assays, circular dichroism, fluorescence, light scattering, and transition metal FRET.

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