A novel type of crystallin in the frog eye lens

Tomarev, Stanislav I.; Zinovieva, R. D.; Dolgilevich, Svetlana M.; Luchin, Sergey V.; Krayev, A.S.; Skryabin, K. G.; Gause, G.G.

doi:10.1016/0014-5793(84)80508-6

Cited by 70 publications

(25 citation statements)

References 16 publications

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“…The primary structure of the predominant bovine P-crystallin chain, PBp, has been elucidated [5], while the protein structure of a major murine P-crystallin polypeptide (P 23) has been deduced from cDNA and genomic DNA analysis [6, 71. Several mRNAs of the rat lens crystallins have been cloned [8], and recently the nucleotide sequence of one of these has revealed the primary structure of the PBlchain (J. T. den Dunnen and J. G. G. Schoenmakers, unpublished data).Amino acid sequence determination of bovine y-crystallins [9, 101 and nucleotide sequence analyses of several y-crystallin cDNAs from rat [ll] and frog [12] have shown a considerable homology between P and y-crystallins. The three-dimensional structure of the bovine y-I1 chain has been determined [13] and a similar tertiary fold has been predicted for two / 3 chains, BBp [I41 and 823 [7].…”

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“…Amino acid sequence determination of bovine y-crystallins [9, 101 and nucleotide sequence analyses of several y-crystallin cDNAs from rat [ll] and frog [12] have shown a considerable homology between P and y-crystallins. The three-dimensional structure of the bovine y-I1 chain has been determined [13] and a similar tertiary fold has been predicted for two / 3 chains, BBp [I41 and 823 [7].…”

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confidence: 99%

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Homology between the primary structures of the major bovine β‐crystallin chains

Berbers

Hoekman

Bloemendal

et al. 1984

European Journal of Biochemistry

114

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Partial amino acid sequences of six major subunits of bovine P-crystallin have been determined by automatic liquid-phase Edman degradation and the dansyl-Edman procedure, complemented by amino acid analyses of peptides. The results show that, including the previously established PBp sequence [H. P. Eur. J. Biochem. 121,, there exist at least seven primary gene products in bovine P-crystallin, which exhibit 40 % or more sequence homology. Two of the gene products are completely identical except for the presence in one of them of 17 additional residues at the N terminus, possibly caused by differential splicing of the same primary RNA transcript. The rate of evolutionary change of the fi chains (4 % sequence change per 100 x lo6 years) is about equally slow as that of a-crystallin, and the gene duplications giving rise to the different chains must have occurred very early in vertebrate evolution. The P chains can be divided into two groups, according to sequence homology and presence of deletions/insertions and C-terminal extension, on which basis a new, rational nomenclature for the /? subunits is introduced. The N-terminal extensions of all P chains are very different in length and sequence, even between homologous P chains in different species. Possible explanations for this finding are discussed.The evolutionarily highly conserved structural eye lens proteins, the crystallins, can be divided into four classes a, P, y and h-crystallin, of which P-crystallin is the most heterogeneous [I]. In bovine P-crystallin six or more chains are primary gene products, whereas some ten others arise by post-translational modification [2]. They can associate to oligomers, varying from dimers and trimers (filow) to octamers (fihigh) [2,3]. This diversity in P-crystallin subunits has also been found at the mRNA level in the chicken lens [4]. The primary structure of the predominant bovine P-crystallin chain, PBp, has been elucidated [5], while the protein structure of a major murine P-crystallin polypeptide (P 23) has been deduced from cDNA and genomic DNA analysis [6, 71. Several mRNAs of the rat lens crystallins have been cloned [8], and recently the nucleotide sequence of one of these has revealed the primary structure of the PBlchain (J. T. den Dunnen and J. G. G. Schoenmakers, unpublished data).Amino acid sequence determination of bovine y-crystallins [9, 101 and nucleotide sequence analyses of several y-crystallin cDNAs from rat [ll] and frog [12] have shown a considerable homology between P and y-crystallins. The three-dimensional structure of the bovine y-I1 chain has been determined [13] and a similar tertiary fold has been predicted for two / 3 chains, BBp [I41 and 823 [7]. The P and y-crystallins are built up of two domains, which show considerable sequence similarity, suggesting an intragenic duplication in the ancestral gene of these proteins. Each of the domains is again folded into two similar 'Greek key' motifs. A relationship between these structural motifs and the exons of the murine P23 gene has been suggeste...

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confidence: 99%

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confidence: 99%

Homology between the primary structures of the major bovine β‐crystallin chains

Berbers

Hoekman

Bloemendal

et al. 1984

European Journal of Biochemistry

114

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“…After submission of this paper the name &-crystallin has also been proposed for a novel 35-kDa lens protein from the frog Rana temporaria, of which protein the partial cDNA sequence has been determined [27]. Apart from the similarity in subunit molecular mass and their oligomeric structure, the presently available data do not seem to support an evolutionary relationship between this frog crystallin and the avian and reptilian &-crystallin described in the present paper and mentioned earlier [13,24,281.…”

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confidence: 62%

ɛ‐Crystallin, a novel avian and reptilian eye lens protein

Stapel

Zweers

Dodemont

et al. 1985

European Journal of Biochemistry

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Gel filtration of Peking duck eye lens proteins reveals a component eluting just behind δ‐crystallin and comprising approximately 10% of the total soluble protein. The native Mr of this additional component is estimated to be 120000; it appears to be composed of three identical chains of Mr 38000 and pl 7.5. Circular dichroic spectroscopy showed a relatively high α‐helical content. No immunological cross‐reactivity is found with α‐, β‐, γ‐ or δ‐crystallins, and partial amino acid sequence determinations likewise failed to reveal any similarity with other known crystallins. We conclude that this protein represents another and novel family of eye lens proteins, for which we propose the designation ɛ‐crystallin. ɛ‐Crystallin is translated from a 1450‐base mRNA, which has been partially purified. ɛ‐Crystallin is found scattered among avian and reptilian taxa, but not in other vertebrates. Its rate of evolutionary change seems to be as slow as that of α‐ and β‐crystallins.

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“…In general, the following superfamilies can be distinguished: (1) aldo-keto reductases comprising human liver aldehyde reductase, human placenta aldose reductase, rat lens aldose reductase [2 1,221, Z,Sdiketogluconic acid reductase [23j, prostaglandin F synthetase [24], and frog p-crystallin [25]; (2) short-chain alcohol dehydrogenases comprising 17/I-hydroxysteroid dehydrogenase, IS-hydroxyprostaglandin dehydrogenase, Nod G protein of Rhkobium rnelilolii [26] and 3p-hydroxysteroid dehydrogenase from Pseudomonas testosteroni [27]; (3) NAD(P):quinone oxidoreductase, hitherto the sole member of this family.…”

Section: Discussionmentioning

confidence: 99%

Functional and immunological relationships between metyrapone reductase from mouse liver microsomes and 3α‐hydroxysteroid dehydrogenase from Pseudomonas testosteroni

et al. 1992

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-HSD) from f?~domor~~s resroslerurri was shown to reduce the xenobiotic carbonyl compound mctyrapone (MPON). Revcrscly, MPON reductase purified from mouse liver microsomcs and previously characterized as aldehyde rcductase, was competitively inhibited by 3o-HSD steroid substrates. For MPON reduction both enzymes can use either NADH or NADPH as co-substrate. lmmunoblot analysis alter native and SDS gel eleclrophoresis of 31x-HSD gave a specific crossreaction with the antibodies against the microsomal mouse liver MPON reductase pointing to structural homologies bctwtin these enzymes. In conclusion, there seem to exist structural as well as functional relationships between a mammalian liver aldehyde reductase and prokaryotic 3a-HSD. Moreover, based on the molecular weights and the co-substrate specificities microsomal mouse liver MPON reductose and Pseudomonas 30.HSD seem to be members of the short-chain alcohol dehydrogenase fumily.

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A novel type of crystallin in the frog eye lens

Cited by 70 publications

References 16 publications

Homology between the primary structures of the major bovine β‐crystallin chains

Homology between the primary structures of the major bovine β‐crystallin chains

ɛ‐Crystallin, a novel avian and reptilian eye lens protein

Functional and immunological relationships between metyrapone reductase from mouse liver microsomes and 3α‐hydroxysteroid dehydrogenase from Pseudomonas testosteroni

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