Gene sharing by delta-crystallin and argininosuccinate lyase.

Piatigorsky, Joram; O’Brien, William E.; Norman, Barbara; Kalumuck, Karen; Wistow, Graeme; Borrás, Teresa; Nickerson, John M.; Wawrousek, Eric F.

doi:10.1073/pnas.85.10.3479

Cited by 254 publications

(198 citation statements)

References 46 publications

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“…Some crystallin promoters are active in all lens cells as well as some non-lens tissues (50,51). In contrast, ␤B1-crystallin transcription is highly lens fiber cell preferred (38,41).…”

Section: Discussionmentioning

confidence: 99%

Mafs, Prox1, and Pax6 Can Regulate Chicken βB1-Crystallin Gene Expression

Cui

Tomarev

Piatigorsky

et al. 2004

Journal of Biological Chemistry

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During lens fiber cell differentiation, the regulation of crystallin gene expression is coupled with dramatic morphological changes. Here we report that Mafs, Prox1, and Pax6, which are essential transcription factors for normal lens development, bind to three functionally important cis elements, PL1, PL2, and OL2, in the chicken ␤B1-crystallin promoter and may cooperatively direct the transcription of this lens fiber cell preferred gene. Gel shift assays demonstrated that Mafs bind to the MARE-like sequences in the PL1 and PL2 elements, whereas Prox1, a sequence-specific DNA-binding protein like its Drosophila homolog Prospero, interacts with the OL2 element. Furthermore, Pax6, a known repressor of the chicken ␤B1-crystallin promoter, binds to all three of these cis elements. In transfection assays, Mafs and Prox1 activated the chicken ␤B1-crystallin promoter; however, their transactivation ability was repressed when co-transfected with Pax6. Taken together with the known spatiotemporal expression patterns of Mafs, Prox1, and Pax6 in the developing lens, we propose that Pax6 occupies and represses the chicken ␤B1-crystallin promoter in lens epithelial cells, and is displaced by Prox1 and Mafs, which activate the promoter, in differentiating cortical fiber cells.

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“…Some crystallin promoters are active in all lens cells as well as some non-lens tissues (50,51). In contrast, ␤B1-crystallin transcription is highly lens fiber cell preferred (38,41).…”

Section: Discussionmentioning

confidence: 99%

Mafs, Prox1, and Pax6 Can Regulate Chicken βB1-Crystallin Gene Expression

Cui

Tomarev

Piatigorsky

et al. 2004

Journal of Biological Chemistry

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“…The puzzling case of the crystallins evoked many attempts to explain this evolutionary phenomena [23]. The most plausible explanations suggest structural conservation, referred to as gene sharing [25]. The domains that are adopted by the crystallins may be preserved because of physical properties of the enzymes, e.g.…”

Section: Discussionmentioning

confidence: 99%

“…The domains that are adopted by the crystallins may be preserved because of physical properties of the enzymes, e.g. their ability to reach high concentrations without precipitation or their thermodynamic properties which predict their stability and a very low turn over [25]. A surprising sequence similarity with no apparent functional conservation was also shown between a synaptic vesicle protein and a family of crystallin/enzyme [27].…”

Section: Discussionmentioning

confidence: 99%

Nucleotide bindind by the synapse associated protein SAP90

Kistner

Garner²,

Linial

1995

FEBS Letters

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The rat synapse associated protein SAP90 is a member of a superfamily of potential guanylate kinases localized at cell-cell contact sites. This superfamily includes the synapse associated protein SAP97, a close relative of SAP90, the Drosophila tumor suppressor gene product dlg-Ap, the mammalian zonula occludens proteins ZO-1 and ZO-2 and the erythrocyte protein p55. Here we show that SAP90 specifically binds GMP in the micromolar range while binding to ATP, GDP and ADP is at a much lower affinity (10-25 mM), whether or not binding is detected for other guanine and adenine nucleotides. No guanylate kinase activity of SAP90 was detected under our experimental conditions. The importance of the GMP binding capacity per se and an evolutionary role for conserving of the guanylate kinase domain in this superfamily are discussed.

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“…Many lens crystallins are either closely related or identical to metabolic enzymes (the enzyme-crystallins) or stress proteins (small heat shock proteins) that are used outside of the lens for non-refractive purposes (7)(8)(9). The dual use of crystallins for metabolism and refraction has been called gene sharing (10).…”

mentioning

confidence: 99%

Evidence for Gelsolin as a Corneal Crystallin in Zebrafish

Kantorow

Davis

et al. 2000

Journal of Biological Chemistry

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We have shown that gelsolin is one of the most prevalent water-soluble proteins in the transparent cornea of zebrafish. There are also significant amounts of actin. In contrast to actin, gelsolin is barely detectable in other eye tissues (iris, lens, and remaining eye) of the zebrafish. Gelsolin cDNA hybridized intensely in Northern blots to RNA from the cornea but not from the lens, brain, or headless body. The deduced zebrafish gelsolin is ϳ60% identical to mammalian cytosolic gelsolin and has the characteristic six segmental repeats as well as the binding sites for actin, calcium, and phosphatidylinositides. In situ hybridization tests showed that gelsolin mRNA is concentrated in the zebrafish corneal epithelium. The zebrafish corneal epithelium stains very weakly with rhodamine-phalloidin, indicating little Factin in the cytoplasm. In contrast, the mouse corneal epithelium contains relatively little gelsolin and stains intensely with rhodamine-phalloidin, as does the zebrafish extraocular muscle. We propose, by analogy with the diverse crystallins of the eye lens and with the putative enzyme-crystallins (aldehyde dehydrogenase class 3 and other enzymes) of the mammalian cornea, that gelsolin and actin-gelsolin complexes act as watersoluble crystallins in the zebrafish cornea and contribute to its optical properties.Focused vision in the vertebrate eye depends upon light transmission through the transparent lens and cornea. The lens is an encapsulated tissue containing a layer of anterior, cuboidal epithelial cells and posterior, elongated fiber cells (1). By contrast, the transparent cornea has an anterior squamous epithelium comprising 5-7 cell layers overlying a relatively thick extracellular stroma containing ordered collagen fibers, proteoglycans, glycosaminoglycans, and keratocytes, and finally a posterior single layer of endothelial cells (2-5).The transparent and refractive properties of the eye lens depend upon the crystallins, which often differ among species in a taxon-specific fashion (6). The diverse crystallins comprise approximately 90% of the water-soluble proteins of the lens. Many lens crystallins are either closely related or identical to metabolic enzymes (the enzyme-crystallins) or stress proteins (small heat shock proteins) that are used outside of the lens for non-refractive purposes (7-9). The dual use of crystallins for metabolism and refraction has been called gene sharing (10).Because transparency of the cellular lens involves the intracellular crystallins (11-13), studies on corneal transparency have concentrated on the highly structured extracellular stroma (14, 15). However, corneal epithelial cells, like lens cells, contain unexpectedly high proportions of selected proteins (16 -19), raising the possibility that they may have structural roles related to transparency as do lens crystallins. Furthermore, these abundant intracellular corneal proteins are often enzymes, reminiscent of the enzyme-crystallins in the lens, suggesting that they are not serving strictly metabolic roles. ...

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Gene sharing by delta-crystallin and argininosuccinate lyase.

Cited by 254 publications

References 46 publications

Mafs, Prox1, and Pax6 Can Regulate Chicken βB1-Crystallin Gene Expression

Mafs, Prox1, and Pax6 Can Regulate Chicken βB1-Crystallin Gene Expression

Nucleotide bindind by the synapse associated protein SAP90

Evidence for Gelsolin as a Corneal Crystallin in Zebrafish

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