Crystallins are a family of proteins primarily known for their role in maintaining the transparency and refractive index of the vertebrate eye lens. They are categorized into two main classes: taxon-specific (or enzyme) crystallins and ubiquitous crystallins. Crystallin Zeta (CRYZ), also known as Zeta-crystallin, belongs to the taxon-specific class and is encoded by the CRYZ gene .
Crystallin Zeta is a protein-coding gene that produces a protein with NADPH-dependent quinone reductase activity. This activity is distinct from other known quinone reductases and does not include alcohol dehydrogenase activity, despite being a member of the zinc-containing alcohol dehydrogenase family . The protein binds NADP and acts through a one-electron transfer process, with orthoquinones such as 1,2-naphthoquinone or 9,10-phenanthrenequinone being the best substrates in vitro .
Crystallin Zeta has two main functions:
Crystallin Zeta has been associated with various diseases, including transitional papilloma and developmental and epileptic encephalopathy 87 . Its role in stabilizing mRNAs encoding proteins involved in renal glutamine catabolism during metabolic acidosis suggests a potential involvement in metabolic regulation and response to cellular stress .
Recombinant human Crystallin Zeta is produced by expressing the CRYZ gene in systems such as E. coli, with the protein often fused to tags (e.g., His-tag) to facilitate purification . This recombinant protein is used in research to study its structure, function, and potential therapeutic applications.