An analysis of intron positions in relation to nucleotides, amino acids, and protein secondary structure.
We present an analysis of intron positions in relation to nucleotides, amino acid residues, and protein secondary structure. Previous work has shown that intron sites in proteins are not randomly distributed with respect to secondary structures. Here we show that this preference can be almost totally explained by the nucleotide bias of splice site machinery, and may well not relate to protein stability or conformation at all. Each intron phase is preferentially associated with its own set of residues: phase 0 introns with lysine, glutamine, and glutamic acid before the intron, and valine after; phase 1 introns with glycine, alanine, valine, aspartic acid, and glutamic acid; and phase 2 introns with arginine, serine, lysine, and tryptophan. These preferences can be explained principally on the basis of nucleotide bias at intron locations, which is in accordance with previous literature. Although this work does not prove that introns are inserted into genomes at specific proto-splice sites, it shows that the nucleotide bias surrounding introns, however it originally occurred, explains the observed correlations between introns and protein secondary structure.
Whamond
Gordon S
GS
Department of Biochemistry and Molecular Biology, University College London, UK. whamond@ebi.ac.uk
Thornton
Janet M
JM
D000596:Amino Acids; D003062:Codon; D030562:Databases, Protein; D007438:Introns; D009711:Nucleotides; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry / Q000235:genetics; D017422:Sequence Analysis, DNA
D000596:Amino Acids; D003062:Codon; D009711:Nucleotides; D011506:Proteins