Evolutionary and structure-function analysis elucidates diversification of prokaryotic and eukaryotic trehalases

Area of Science:

• Biochemistry
• Evolutionary Biology
• Genomics

Background:

• Trehalase catalyzes trehalose breakdown into glucose, an essential enzyme found across diverse organisms.
• Understanding the evolutionary trajectory of trehalase is crucial for comprehending its functional diversification.

Purpose of the Study:

• To investigate the origin and evolutionary history of trehalase in major species.
• To elucidate the molecular mechanisms underlying trehalase adaptation and functional divergence.

Main Methods:

• Phylogenetic analysis and orthology studies to trace evolutionary relationships.
• Functional domain analysis to identify conserved and variable regions.
• Gene context and selection pressure analyses to infer evolutionary pressures and functional constraints.

Main Results:

• Evidence suggests trehalase originated in bacteria and was disseminated through horizontal gene transfer.
• Glycosyl hydrolase family 37 is a dominant feature, indicating its ancient role; cytosolic trehalase predates transmembrane forms.
• Domain rearrangements were observed, facilitating adaptation to environmental challenges like acidic pH.
• Gene neighborhood analysis reveals links to sugar transport and lipid metabolism, suggesting coordinated regulation.
• Evolutionary analyses show gene duplication and purifying selection, with conserved functionally important residues.

Conclusions:

• Trehalase's evolutionary path involves bacterial origins, horizontal gene transfer, and adaptive domain modifications.
• The enzyme's structure and function are shaped by selection pressures, leading to conserved active sites and specialized adaptations like acid tolerance.