Recruitment of enzymes as lens structural proteins.

@article{Wistow1987RecruitmentOE,
  title={Recruitment of enzymes as lens structural proteins.},
  author={Graeme Wistow and Joram Piatigorsky},
  journal={Science},
  year={1987},
  volume={236 4808},
  pages={
          1554-6
        }
}
Crystallins, the principal components of the lens, have been regarded simply as soluble, structural proteins. It now appears that the major taxon-specific crystallins of vertebrates and invertebrates are either enzymes or closely related to enzymes. In terms of sequence similarity, size, and other physical characteristics delta-crystallin is closely related to argininosuccinate lyase, tau-crystallin to enolase, and SIII-crystallin to glutathione S-transferase; moreover, it has recently been… Expand
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It appears that an active enzyme has been recruited, unchanged, to an extra role as a structural protein in the lens without gene duplication and sequence divergence, which raises the possibility that other crystallins may similarly be enzymes expressed at high levels in lens as structural proteins. Expand
Domain structure and evolution in α‐crystallins and small heat‐shock proteins
Lu-Crystallin is an evolutionarily conserved, highly stable, structural protein of the eye lens [1,2]. A region covering over 50% of the subunit amino acid sequences of both the bovine (YcrystallinExpand
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The main water-soluble proteins of squid lens (S-crystallins) have a molecular weight of 60 000, a sedimentation coefficient s020,w of 5.2 S, 20-30% alpha-helical secondary structure, and anExpand
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Abstract A lens protein with a molecular mass near 46 000 daltons has been purified from the turtle lens. It is a monomeric protein which differs from other lens cyrstallins in its antigenicity,Expand
Myxococcus xanthus spore coat protein S may have a similar structure to vertebrate lens βγ-crystallins
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In order to understand how crystallin genes are regulated so that they would be expressed with a high lens specificity, we introduced a cloned delta-crystallin gene of the chicken and its derivativesExpand
Yeast heat-shock protein of Mr 48,000 is an isoprotein of enolase
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The three-dimensional structure of the eye lens protein, bovine γ-crystallin II, has been determined at 2.6 Å resolution. The protein has a two domain β-structure, folded into four remarkably similarExpand
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TLDR
Analysis of the deduced delta-crystallin protein using a program which accounts for conservative amino acid changes shows regions of similarity within the delta 1 amino acid sequence which suggest a rough 2-fold repeat in the protein structure. Expand
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