Ethylnitrosourea-Induced Mutation in Mice Leads to the Expression of a Novel Protein in the Eye and to Dominant Cataracts
| Autor: | Eckhard Wolf, Helmut Fuchs, Dian Soewarto, André Reis, Martin Hrabé de Angelis, Rudi Balling, N Klopp, Johannes Becker-Follmann, Jana Löster, Jochen Graw |
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| Rok vydání: | 2001 |
| Předmět: |
Genetic Markers
Male Blotting Western Molecular Sequence Data Mutant Biology Eye medicine.disease_cause Polymerase Chain Reaction Cataract Mice Open Reading Frames Start codon Crystallin Sequence Homology Nucleic Acid Lens Crystalline Gene cluster Genetics medicine Animals Amino Acid Sequence Codon crystallin gene gamma-crystallins mouse evolution mutant Peptide sequence Gene Crosses Genetic Mutation Base Sequence Models Genetic Crystallins Molecular biology eye diseases Open reading frame Haplotypes Electrophoresis Polyacrylamide Gel Female sense organs Software Mutagens Research Article |
| Zdroj: | Scopus-Elsevier ResearcherID Genetics 157, 1313-1320 (2001) Europe PubMed Central |
| ISSN: | 1943-2631 |
| DOI: | 10.1093/genetics/157.3.1313 |
| Popis: | A novel ENU-induced mutation in the mouse leading to a nuclear and zonular opacity of the eye lens (Aey1) was mapped to chromosome 1 between the markers D1Mit303 and D1Mit332. On the basis of the chromosomal position, the γ-crystallin encoding gene cluster (Cryg) and the βA2-crystallin encoding gene Cryba2 were tested as candidate genes. An A → T mutation destroys the start codon of the Cryge gene in the mutants; this mutation was confirmed by the absence of a restriction site for NcoI in the corresponding genomic fragment of homozygous mutants. The next in-frame start codon is 129 bp downstream; this predicted truncated γE-crystallin consists of 131 amino acids, resulting in a molecular mass of 14 kD. However, another open reading frame was observed just 19 bp downstream of the regular Cryge start codon, resulting in a protein of 119 amino acids and a calculated molecular weight of 13 kD. Western blot analysis using polyclonal antibodies against γ-crystallins or the novel Aey1-specific protein demonstrated the specific expression of the Aey1 protein in the cataractous lenses only; the truncated form of the γE-crystallin could not be detected. Therefore, it is concluded that the novel protein destroys the sensitive cellular structure of the eye lens. |
| Databáze: | OpenAIRE |
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