ζ‐Crystallin versus other members of the alcohol dehydrogenase super‐family Variability as a functional characteristic

@article{Jrnvall1993CrystallinVO,
  title={$\zeta$‐Crystallin versus other members of the alcohol dehydrogenase super‐family Variability as a functional characteristic},
  author={Hans J{\"o}rnvall and Bengt Persson and Garrett C. Du Bois and Gene C. Lavers and John Chen and Pedro Gonzalez and Ponugoti Vasantha Rao and J. Samuel Zigler},
  journal={FEBS Letters},
  year={1993},
  volume={322}
}

Kinetic and structural evidence of the alkenal/one reductase specificity of human ζ-crystallin

The X-ray structure of ζ-crystallin is reported, which represents the first structure solved for a tetrameric Zn2+-lacking MDR, and which allowed the identification of the active-site lining residues.

A Super‐Family of Medium‐Chain Dehydrogenases/Reductases (MDR): Sub‐Lines including ζ‐Crystallin, Alcohol and Polyol Dehydrogenases, Quinone Oxidoreductases, Enoyl Reductases, VAT‐1 and other Proteins

A distant origin and divergent functions, but related forms and interactions, appear to apply to the entire chains of the many prokaryotic and eukaryotic members.

The alcohol dehydrogenase system.

The SDR family includes the Drosophila alcohol dehydrogenase, which has shorter subunits, no similar metal requirements, other sub-domain arrangements with different structural relationships, and other subunit interactions.

A super-family of medium-chain dehydrogenases/reductases (MDR). Sub-lines including zeta-crystallin, alcohol and polyol dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and other proteins.

A distant origin and divergent functions, but related forms and interactions, appear to apply to the entire chains of the many prokaryotic and eukaryotic members.

Human and yeast ζ-crystallins bind AU-rich elements in RNA

The human and yeast enzymes specifically bind to adenine-uracil rich elements (ARE) in RNA, indicating that both enzymes are ARE-binding proteins and that this property has been conserved in ζ-crystallins throughout evolution.

Evidence for independent recruitment of zeta-crystallin/quinone reductase (CRYZ) as a crystallin in camelids and hystricomorph rodents.

The data presented here show that in both species such recruitment most likely occurred through the generation of new lens promoters from nonfunctional intron sequences by the accumulation of point mutations and/or small deletions and insertions, which support the idea that recruitment of CRYZ resulted from an adaptive process in which the high expression ofCRYZ in the lens provides some selective advantage rather than from a purely neutral evolutionary process.

Comparative analysis of the zeta-crystallin/quinone reductase gene in guinea pig and mouse.

This is the first example in which the recruitment of an enzyme as a lens crystallin can be explained by the acquisition of an alternative lens-specific promoter, and the presence of two promoters in the guinea pig zeta-crystallin gene, one responsible for expression at enzymatic levels and the other responsible for the high expression in the lens.

The yeast ζ‐crystallin/NADPH:quinone oxidoreductase (Zta1p) is under nutritional control by the target of rapamycin pathway and is involved in the regulation of argininosuccinate lyase mRNA half‐life

It is proposed that Zta1p participates in the post‐transcriptional regulation of ARG4 expression by increasing the ARG3 mRNA half‐life and shed new light on the ζ‐crystallin family members from yeast to humans as stress response proteins with a bifunctional role in the detoxification of alkenal and alkenone compounds, and the regulation of gene expression.

Human carbonyl reductases.

The present review summarizes the current knowledge on these enzymes with special emphasis on their role as a defence system against toxicants, as well as their possible physiological function and medical application and their possible association with cancer.

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The major alcohol dehydrogenase of cod liver has been purified, enzymatically characterized, and structurally analyzed in order to establish original functions and relationships among the deviating

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The conservation of the stable parts of the fold, the absence of the loop structure, the lack of the metal atoms, and the presence of only a small proportion of oxidation-sensitive cysteine residues in crystallin suggest an increased stability of the lens protein and a derivation from the alcohol dehydrogenase family.

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It now appears that the major taxon-specific crystallins of vertebrates and invertebrates are either enzymes or closely related to enzymes.

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