Tau-crystallin/alpha-enolase: one gene encodes both an enzyme and a lens structural protein

@article{Wistow1988TaucrystallinalphaenolaseOG,
  title={Tau-crystallin/alpha-enolase: one gene encodes both an enzyme and a lens structural protein},
  author={Graeme Wistow and T Lietman and Leah A. Williams and Steven O. Stapel and Wilfried W. de Jong and Joseph Horwitz and Joram Piatigorsky},
  journal={The Journal of Cell Biology},
  year={1988},
  volume={107},
  pages={2729 - 2736}
}
tau-Crystallin has been a major component of the cellular lenses of species throughout vertebrate evolution, from lamprey to birds. Immunofluorescence analysis of the embryonic turtle lens, using antiserum to lamprey tau-crystallin showed that the protein is expressed throughout embryogenesis and is present at high concentrations in all parts of the lens. Partial peptide sequence for the isolated turtle protein and deduced sequences for several lamprey peptides all revealed a close similarity… Expand
Cloning and sequencing of complete tau-crystallin cDNA from embryonic lens of Crocodylus palustris.
TLDR
The cloning and sequencing of complete tau-crystallin cDNA from the embryonic lens of Crocodylus palustris are presented and it is established to be identical to the a-enolase gene from non-lenticular tissues, suggesting both to be the product of the same gene. Expand
Structure and expression of the duck α-enolase/τ-crystallin-encoding gene
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It is reported that duck α ENO/τCRY mRNA levels are developmentally regulated; αENO/ τCRY RNA levels in the lens increase over those in the liver by embryonic day 14 and, within the lens, are higher in the Lens epithelium than in fiber cells. Expand
Structure and expression of the scallop Omega-crystallin gene. Evidence for convergent evolution of promoter sequences.
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The cloned scallop Omega-crystallin gene suggests convergent evolutionary adaptations that underlie the preferential expression of crystallin genes in the lens of vertebrates and invertebrates. Expand
Cloning and sequencing of complete τ-crystallin cDNA from embryonic lens ofCrocodylus palustris
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The cloning and sequencing of complete τ-crystallin cDNA from the embryonic lens of crocodile are presented and it is established to be identical to the α-enolase gene from non-lenticular tissues, suggesting both to be the product of the same gene. Expand
Gene conversion and splice-site slippage in the argininosuccinate lyases/delta-crystallins of the duck lens: members of an enzyme superfamily.
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Protein Expression and Purification
t -Crystallin is a taxon-restricted crystallin found in eye lenses of reptiles and a few avian species but presumably absent in mammals. The level of t -crystallin in the lens varies among differentExpand
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The ubiquitous α-crystallin genes may provide some insight into the mechanisms used to recruit metabolic enzymes as taxon-specific lens crystallins. Expand
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Structural analysis of alpha-enolase. Mapping the functional domains involved in down-regulation of the c-myc protooncogene.
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Anomalous behavior of beta B1-crystallin subunits from avian lenses.
TLDR
It is shown that, in spite of high conservation in primary sequence, beta B1-crystallin subunits of avian lenses have a markedly slower migration in SDS PAGE than those of mammals and that the apparent subunit size of beta B 1- Crystallin varies among birds. 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
epsilon-Crystallin, a novel avian and reptilian eye lens protein.
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Epsilon-Crystallin is a novel family of eye lens proteins found scattered among avian and reptilian taxa, but not in other vertebrates, and its rate of evolutionary change seems to be as slow as that of alpha- and beta-crystallins. Expand
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Molecular modeling of LDH-B sequences shows that the increased thermostability of the avian tetramer might be explained by mutations that increase the number of ion pairs, and the replacement of bulky side chains by glycines on the corners of the duck protein suggests an adaptation to facilitate close packing in the lens. Expand
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TLDR
expression of the gamma-crystallin coding sequences from the human metallothionein IIA promoter in nonlens cells facilitated characterization of the polypeptides encoded by individual gamma-genes and should permit comparison of these proteins with distinct gamma- Crystallins in the human lens. Expand
Ontogeny of the 35K epsilon crystallin during Rana temporaria lens development.
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The purity of the isolated 35K protein and the specificity of the antibody were controlled by Tris-SDS gel electrophoresis and immuno-blotting, respectively and the first positive immunofluorescence reaction was observed in the inner cell wall of a stage V lens. Expand
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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. Expand
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TLDR
The data indicate that the same gene, at least in ducks, encodes two different functions, an enzyme (ASL) and a structural protein (delta-crystallin), although in chickens specialization and separation of functions may have occurred. Expand
δ- and β-crystallin mRNA levels in the embryonic and posthatched chicken lens: Temporal and spatial changes during development
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These experiments provide a quantitative basis for exploring the differential expression of the δ- and β-crystallin gene families in the chicken lens and differentially regulated in cultured embryonic lens epithelia. Expand
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