Work

Characterizing selective pressures on the pathway for de novo biosynthesis of pyrimidines in yeast

Year: 2015

Type: article

Abstract: BACKGROUND: Selection on proteins is typically measured with the assumption that each protein acts independently. However, selection more likely acts at higher levels of biological organization, requiring an integrative view of protein function. Here, we built a kinetic model for de novo pyrimidine biosynthesis in the yeast Saccharomyces cerevisiae to relate pathway function to selective pressures on individual protein-encoding genes. RESULTS: Gene families across yeast were constructed for each member of the pathway and the ratio of nonsynonymous to synonymous nucleotide substitution rates (dN/dS) was estimated for each enzyme from S. cerevisiae and closely related species. We found a positive relationship between the influence that each enzyme has on pathway function and its selective constraint. CONCLUSIONS: We expect this trend to be locally present for enzymes that have pathway control, but over longer evolutionary timescales we expect that mutation-selection balance may change the enzymes that have pathway control.

Source: BMC Evolutionary Biology

DOI: 10.1186/s12862-015-0515-x

Authors: Russell A. Hermansen, Brian K. Mannakee, Wolfgang Knecht, David A. Liberles, Ryan N. Gutenkunst

Institutions: University of Wyoming, Temple University, University of Arizona, Lund University

Language: English

Topic: Evolution and Genetic Dynamics

Subfield: Genetics

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: gold

Estimated APC paid: $2,290

Funder: National Science Foundation