Functional significance may underlie the taxonomic utility of single amino acid substitutions in conserved proteins.

ABSTRACT: We hypothesized that some amino acid substitutions in conserved proteins that are strongly fixed by critical functional roles would show lineage-specific distributions. As an example of an archetypal conserved eukaryotic protein we considered the active site of beta-tubulin. Our analysis identified one amino acid substitution--beta-tubulin F224--which was highly lineage specific. Investigation of beta-tubulin for other phylogenetically restricted amino acids identified several with apparent specificity for well-defined phylogenetic groups. Intriguingly, none showed specificity for "supergroups" other than the unikonts. To understand why, we analysed the beta-tubulin Neighbor-Net and demonstrated a fundamental division between core beta-tubulins (plant-like) and divergent beta-tubulins (ani

SUBMITTER: Tyler KM 

PROVIDER: S-EPMC2874023 | biostudies-literature | 2010 Apr

REPOSITORIES: biostudies-literature