Chicken Vigilin Gene organization and expression pattern

• Published in: European journal of biochemistry Vol. 209; no. 1; pp. 321 - 328
• Main Authors: HENKEL, Barbara, SCHMIDT, Cornelia, ZORBAS, Haralabos, PÖSCHL, Ernst, GLOE, Torsten R., PURSCHKE, Werner G., MÜLLER, Peter K.
• Format: Journal Article
• Language: English
• Published: Oxford, UK Blackwell Publishing Ltd 01.10.1992
• ISSN: 0014-2956; 1432-1033
• DOI: 10.1111/j.1432-1033.1992.tb17292.x

Chicken vigilin was identified as a member of an evolutionary‐conserved protein family with a unique repetitive domain structure. 14 tandemly repeated domains are found in chicken vigilin, all of which consist of a conserved sequence motif (subdomain A) and a potential α‐helical region (subdomain B) [1]. We have established the physical structure of the chicken vigilin gene by restriction‐fragment analysis and DNA sequencing of overlapping clones isolated from a phage λ genomic DNA library. The chicken vigilin gene is a single‐copy gene with a total of 27 exons which are distributed over a region of some 22 kbp. Exon 1 codes for a portion of the 5′ untranslated region, exon 2 contains the translation start point and forms, along with exons 3 and 4, the N‐terminal non‐domain region. Exons 5–25 encode the vigilin domains 1–14 and the remaining exons 26 and 27 contain the non‐domain C‐terminal as well as the untranslated regions. The domain structure of the protein is reflected in the positioning of introns which demarcate individual domains. While domains 1–3 and 8–10 are each encoded by a single exon (5–7, 16–18); all other domains are contained in a set of two exons which are separated by introns interspersed at variable positions of the DNA segment coding for the conserved sequence motif. In conclusion, the data presented suggest that the chicken vigilin gene evolved by amplification of a primordial exon unit coding for the fundamental bipartite vigilin domain.