beta s-Crystallin: structure and evolution of a distinct member of the beta gamma-superfamily.

Quaxjeuken, Y; Driessen, H.P.C.; Leunissen, Jack A. M.; Quax, Wim J.; Jong, Wouter de; Bloemendal, H.

doi:10.1002/j.1460-2075.1985.tb03976.x

Cited by 73 publications

(52 citation statements)

References 38 publications

(32 reference statements)

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“…Crystallins have been observed previously in lenses of the mole rat, S. ehrenbergi, by immunofluorescence (29). In addition, mole rat shsp͞␣B-crystallin, which is 90% identical to that of other mammals, has been detected in the eye and other tissues by reverse transcription-PCR (30).…”

Section: ␣-mentioning

confidence: 77%

Adaptive evolution of small heat shock protein/ αB-crystallin promoter activity of the blind subterranean mole rat,Spalax ehrenbergi

Hough

Avivi

Davis

et al. 2002

Proc. Natl. Acad. Sci. U.S.A.

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Blind mole rats have degenerated subcutaneous eyes that are visually nonfunctional. In this investigation, we have compared the tissue specificity of the small heat shock protein (shsp)͞␣B-crystallin promoter of the mole rat superspecies, Spalax ehrenbergi, with that of the mouse. Earlier experiments showed that mouse shsp͞ ␣B-crystallin promoter͞enhancer activity is high in the lens and moderate in the heart and skeletal muscle of transgenic mice. Here, we show in transgenic mouse experiments using the firefly luciferase reporter gene that, despite relatively few changes in sequence, the mole rat shsp͞␣B-crystallin promoter͞enhancer has selectively lost lens activity after 13.5 days of embryogenesis (E13.5). The ratios of mole rat͞mouse promoter activity were 0.01 for lens, 1.7 for heart, and 13.6 for skeletal muscle in 8-wk-old transgenic mice. Our data indicate that the shsp͞␣B-crystallin promoter͞enhancer has undergone adaptive changes corresponding to the subterranean evolution of the blind mole rat. We speculate that selective pressures on metabolic economy may have contributed to these tissue-specific modifications of promoter͞ enhancer function during adaptation to life underground.

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Section: ␣-mentioning

confidence: 77%

Adaptive evolution of small heat shock protein/ αB-crystallin promoter activity of the blind subterranean mole rat,Spalax ehrenbergi

Hough

Avivi

Davis

et al. 2002

Proc. Natl. Acad. Sci. U.S.A.

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“…In terms of sequence and structure, ␥S is an outlying member of the ␥-crystallin family, and it has been suggested that it might represent a hypothetical ancestor of the ␥-crystallins, possibly predating their recruitment to the lens (35,48,49). This family in turn belongs to the wider ␤␥-crystallin superfamily, which has members in both prokaryotes and eukaryotes (14,50,51).…”

Section: Discussionmentioning

confidence: 99%

A Temperature-sensitive Mutation of Crygs in the Murine Opj Cataract

Sinha

Wyatt

Sarra

et al. 2001

Journal of Biological Chemistry

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In Opj, an inherited cataract in mice, opacity is associated with a mutation in Crygs, the gene for ␥S-crystallin, the first mutation to be associated with this gene. A single base change causes replacement of Phe-9, a key hydrophobic residue in the core of the N-terminal domain, by serine. Despite this highly non-conservative change, mutant protein folds normally at low temperature. However, it exhibits a marked, concentration-dependent decrease in solubility, associated with loss of secondary structure, at close to physiological temperatures. This is reminiscent of processes thought to occur in human senile cataracts in which normal proteins become altered and aggregate. The Opj cataract is progressive and more severe in Opj/Opj than in Opj/؉. Lens histology shows that whereas fiber cell morphology in Opj/؉ mice is essentially normal, in Opj/Opj, cortical fiber cell morphology and the loss of maturing fiber cell nuclei are both severely disrupted from early stages. This may indicate a loss of function of ␥S-crystallin which would be consistent with ideas that members of the ␤␥-crystallin superfamily may have roles associated with maintenance of cytoarchitecture.

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“…Using the computer graphics program FRODO (Jones, 1978), bovine yS-crystallin has already been modeled based on the coordinates of bovine yB-crystallin (Quax-Jeuken et al, 1985).…”

mentioning

confidence: 99%

Three‐dimensional model and quaternary structure of the human eye lens protein γS‐crystallin based on β‐ and γ‐crystallin X‐ray coordinates and ultracentrifugation

et al. 1994

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A 3-dimensional model of the human eye lens protein yS-crystallin has been constructed using comparative modeling approaches encoded in the program COMPOSER on the basis of the 3-dimensional structure of y-crystallin and 0-crystallin. The model is biased toward the monomeric yB-crystallin, which is more similar in sequence. Bovine yS-crystallin was shown to be monomeric by analytical ultracentrifugation without any tendency to form assemblies up to concentrations in the millimolar range. The connecting peptide between domains was therefore built assuming an intramolecular association as in the monomeric y-crystallins. Because the linker has 1 extra residue compared with yB and PB2, the conformation of the connecting peptide was constructed by using a fragment from a protein database. yS-crystallin differs from yB-crystallin mainly in the interface region between domains. The charged residues are generally paired, although in a different way from both 0-and y-crystallins, and may contribute to the different roles of these proteins in the lens.

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beta s-Crystallin: structure and evolution of a distinct member of the beta gamma-superfamily.

Cited by 73 publications

References 38 publications

Adaptive evolution of small heat shock protein/ αB-crystallin promoter activity of the blind subterranean mole rat,Spalax ehrenbergi

Adaptive evolution of small heat shock protein/ αB-crystallin promoter activity of the blind subterranean mole rat,Spalax ehrenbergi

A Temperature-sensitive Mutation of Crygs in the Murine Opj Cataract

Three‐dimensional model and quaternary structure of the human eye lens protein γS‐crystallin based on β‐ and γ‐crystallin X‐ray coordinates and ultracentrifugation

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