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In silico Comparative Analysis of DNA and Amino Acid Sequences for Prion Protein Gene
Author(s) -
Kim Y.,
Lee J.,
Lee C.
Publication year - 2008
Publication title -
transboundary and emerging diseases
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.392
H-Index - 63
eISSN - 1865-1682
pISSN - 1865-1674
DOI - 10.1111/j.1865-1682.2007.00997.x
Subject(s) - biology , genetics , polyadenylation , gene , in silico , intron , conserved sequence , peptide sequence , prnp , untranslated region , gene isoform , sequence analysis , rna , allele
Summary Genetic variability might contribute to species specificity of prion diseases in various organisms. In this study, structures of the prion protein gene ( PRNP ) and its amino acids were compared among species of which sequence data were available. Comparisons of PRNP DNA sequences among 12 species including human, chimpanzee, monkey, bovine, ovine, dog, mouse, rat, wallaby, opossum, chicken and zebrafish allowed us to identify candidate regulatory regions in intron 1 and 3′‐untranslated region (UTR) in addition to the coding region. Highly conserved putative binding sites for transcription factors, such as heat shock factor 2 (HSF2) and myocite enhancer factor 2 (MEF2), were discovered in the intron 1. In 3′‐UTR, the functional sequence (ATTAAA) for nucleus‐specific polyadenylation was found in all the analysed species. The functional sequence (AT) for maturation‐specific polyadenylation was identically observed only in ovine, and one or two nucleotide mismatches in the other species. A comparison of the amino acid sequences in 53 species revealed a large sequence identity. Especially the octapeptide repeat region was observed in all the species but frog and zebrafish. Functional changes and susceptibility to prion diseases with various isoforms of prion protein could be caused by numeric variability and conformational changes discovered in the repeat sequences.