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Updated: Jun 18, 2025
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Applications of pHluorin for Quantitative, Kinetic and High-throughput Analysis of Endocytosis in Budding Yeast
Published on: October 23, 2016
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Specialization restricts the evolutionary paths available to yeast sugar transporters
Johnathan G Crandall1, Xiaofan Zhou2,3, Antonis Rokas3
1Laboratory of Genetics, J. F. Crow Institute for the Study of Evolution, Center for Genomic Science Innovation, DOE Great Lakes Bioenergy Research Center, Wisconsin Energy Institute, University of Wisconsin-Madison, Madison, WI 53726, USA.
Biorxiv : the Preprint Server for Biology
|August 2, 2024
Summary
Protein evolution drives novelty through complex interactions within sugar transporters. Yeast evolution reveals how ancestral multifunctional proteins subfunctionalize, enabling new substrate transport via accumulated genetic changes.
Area of Science:
- Protein evolution
- Molecular biology
- Yeast genetics
Background:
- Functional innovation in proteins is crucial for evolutionary novelties.
- The Major Facilitator Superfamily (MFS) includes diverse sugar porters, known for plasticity.
- Understanding sequence-function relationships is key for evolutionary insights and protein engineering.
Purpose of the Study:
- Investigate the molecular basis of novel function in MFS sugar porters.
- Dissect the evolution of α-glucoside transport in *Saccharomyces eubayanus*.
- Reconcile functional diversity with constrained evolution in this protein family.
Main Methods:
- Dissecting evolutionary innovation in an α-glucoside transporter.
- Generating genome annotations for 332 Saccharomycotina yeast species.
- Integrating phylogenetic and phenotypic analyses.
Main Results:
- Novel substrate transport requires high-order interactions among protein regions and residues near the transport channel.
- Yeast α-glucoside transporters likely evolved from multifunctional ancestors via subfunctionalization.
- Additive and epistatic substitutions entrenched subfunctions, favoring multi-substitution paths to novelty.
Conclusions:
- Protein functional innovation is constrained by specific molecular histories and epistasis.
- Subfunctionalization and accumulated genetic changes shape protein evolution.
- Understanding these evolutionary paths aids in protein engineering and understanding biological diversity.
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