Complete cDNA sequence of chicken vigilin, a novel protein with amplified and evolutionary conserved domains

• Published in: European journal of biochemistry Vol. 206; no. 3; pp. 625 - 634
• Main Authors: SCHMIDT, Cornelia, HENKEL, Barbara, PÖSCHL, Ernst, ZORBAS, Haralabos, PURSCHKE, Werner G., GLOE, Torsten R., MÜLLER, Peter K.
• Format: Journal Article
• Language: English
• Published: Oxford, UK Blackwell Publishing Ltd 15.06.1992; Blackwell
• Subjects: Amino Acid Sequence; Animals; Base Sequence; Biological and medical sciences; Blotting, Northern; Carrier Proteins; Cartilage - chemistry; Cartilage - embryology; Cells, Cultured; Chick Embryo; Chickens - genetics; Cloning, Molecular; DNA - chemistry; Fundamental and applied biological sciences. Psychology; Humans; Molecular and cellular biology; Molecular genetics; Molecular Sequence Data; Proteins - chemistry; Proteins - genetics; Repetitive Sequences, Nucleic Acid; RNA, Messenger - genetics; RNA, Messenger - isolation & purification; RNA-Binding Proteins; Saccharomyces cerevisiae - chemistry; Sequence Homology, Nucleic Acid; Transcription, Genetic; Transcription. Transcription factor. Splicing. Rna processing; 5' terminal-Sequence; Vertebrata; Messenger RNA; Chondrocyte; Complementary DNA; Nucleotide sequence; Sequence alignment; Chicken; Aves; Transcription initiation
• ISSN: 0014-2956; 1432-1033
• DOI: 10.1111/j.1432-1033.1992.tb16967.x

The complete cDNA (4375 bp), coding for a new protein called vigilin, was isolated from chicken chondrocytes. The cDNA shows an open reading frame of 1270 amino acids which are organized in 14 tandemly repeated homologous domains. Each domain consists of two subdomains, one with a conserved sequence motif of 35 amino acids (subdomain A) and another one with a presumptive α‐helical structure of 21–33 amino acids (subdomain B). 149 amino acids at the N‐terminus and 71 amino acids at the C‐terminus of vigilin do not show the characteristic domain structure. No sequence characteristic of a signal peptide has been found, which argues for an intracellular localisation of vigilin. Vigilin is highly expressed in freshly isolated chicken chondrocytes but little in chondrocytes after prolonged time in culture. Vigilin mRNA exists in two size species, 4.4 kb and 6.5 kb in length due to the usage of different polyadenylation sites. Comparison of the vigilin sequence with data bases showed a remarkable similarity to protein HX from Saccharomyces cerevisiae [Delahodde, A., Becam, A. M., Perea, J. & Jacq, C. (1986) Nucleic Acids Res. 14, 9213–9214]. The yeast protein consists of eight homologous domains with 11 conserved amino acid residues within a set of 35 amino acids. The N‐terminal and C‐terminal regions of vigilin and protein HX do not reveal any sequence similarity. These results, together with the demonstration of the characteristic vigilin sequence motif in a human cDNA clone, suggest that the repeats represent evolutionary conserved autonomous domains within a family of proteins found in yeast, chicken and man.