Gene duplication and separation of functions in alphaB-crystallin from zebrafish (Danio rerio)
| العنوان: | Gene duplication and separation of functions in alphaB-crystallin from zebrafish (Danio rerio) |
|---|---|
| المؤلفون: | Graeme Wistow, Jennifer Vacha, Mason Posner, Keith Wyatt, Thomas S. Vihtelic, Amber A. Smith, J. S. Zigler |
| المصدر: | FEBS Journal. 273:481-490 |
| بيانات النشر: | Wiley, 2006. |
| سنة النشر: | 2006 |
| مصطلحات موضوعية: | Time Factors, animal structures, Molecular Sequence Data, Danio, Biology, Biochemistry, Article, Lens protein, Crystallin, Gene Duplication, Gene duplication, Animals, Humans, Electrophoresis, Gel, Two-Dimensional, Amino Acid Sequence, Cloning, Molecular, Molecular Biology, Zebrafish, Phylogeny, Genetics, Regulation of gene expression, Reverse Transcriptase Polymerase Chain Reaction, Alternative splicing, Temperature, Protein primary structure, alpha-Crystallin B Chain, Cell Biology, biology.organism_classification, eye diseases, Cell biology, Alternative Splicing, Gene Expression Regulation, Electrophoresis, Polyacrylamide Gel, sense organs, Sequence Alignment |
| الوصف: | We previously reported that zebrafish alphaB-crystallin is not constitutively expressed in nervous or muscular tissue and has reduced chaperone-like activity compared with its human ortholog. Here we characterize the tissue expression pattern and chaperone-like activity of a second zebrafish alphaB-crystallin. Expressed sequence tag analysis of adult zebrafish lens revealed the presence of a novel alpha-crystallin transcript designated cryab2 and the resulting protein alphaB2-crystallin. The deduced protein sequence was 58.2% and 50.3% identical with human alphaB-crystallin and zebrafish alphaB1-crystallin, respectively. RT-PCR showed that alphaB2-crystallin is expressed predominantly in lens but, reminiscent of mammalian alphaB-crystallin, also has lower constitutive expression in heart, brain, skeletal muscle and liver. The chaperone-like activity of purified recombinant alphaB2 protein was assayed by measuring its ability to prevent the chemically induced aggregation of alpha-lactalbumin and lysozyme. At 25 degrees C and 30 degrees C, zebrafish alphaB2 showed greater chaperone-like activity than human alphaB-crystallin, and at 35 degrees C and 40 degrees C, the human protein provided greater protection against aggregation. 2D gel electrophoresis indicated that alphaB2-crystallin makes up approximately 0.16% of total zebrafish lens protein. Zebrafish is the first species known to express two different alphaB-crystallins. Differences in primary structure, expression and chaperone-like activity suggest that the two zebrafish alphaB-crystallins perform divergent physiological roles. After gene duplication, zebrafish alphaB2 maintained the widespread protective role also found in mammalian alphaB-crystallin, while zebrafish alphaB1 adopted a more restricted, nonchaperone role in the lens. Gene duplication may have allowed these functions to separate, providing a unique model for studying structure-function relationships and the regulation of tissue-specific expression patterns. |
| تدمد: | 1742-4658 1742-464X |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bb85b68179dc00fa15ee0eef673b88e6 https://doi.org/10.1111/j.1742-4658.2005.05080.x |
| حقوق: | OPEN |
| رقم الأكسشن: | edsair.doi.dedup.....bb85b68179dc00fa15ee0eef673b88e6 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 17424658 1742464X |
|---|