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Evolutionary and structure-function analysis elucidates diversification of prokaryotic and eukaryotic trehalases.
J Biomol Struct Dyn. 2019 Jul; 37(11):2926-2937.JB

Abstract

Trehalase catalyses the breakdown of trehalose into two glucose moieties and is ubiquitous in all organisms. Here, we provide insights into the enigmatic origin and evolution of trehalase in major species. Study of taxonomic distribution, orthology, phylogeny and functional domains indicated that trehalase possibly originates from bacteria and was transmitted to other taxa through horizontal gene transfer. Domain analysis showed that glycosyl hydrolase family 37 is present in most of the sequences and represents dominant activity during evolution, and also, illustrating that cytosolic trehalase is primitive than its transmembrane form. Furthermore, it was observed that trehalase went through domain rearrangement to facilitate its activity in adverse environmental conditions like acidic pH. Gene context analysis depicts that trehalase neighbourhood consists of sugar transport and lipid metabolism genes. This highlights their relatedness in metabolic activity and similarity in gene regulation, respectively. Evolutionary and selection pressure analysis demonstrated that trehalase genes were duplicated and evolved under purifying selection, following horizontal gene transfer. Moreover, site-specific rate of evolution emphasized conservation of functionally important residues. In comparison with acid trehalase, neutral trehalase has an extra N-terminal extension. This study serves as an instigation to understand evolution and functionality of trehalase across diverse species. Communicated by Ramaswamy H. Sarma.

Authors+Show Affiliations

a Institute of Bioinformatics and Biotechnology , Savitribai Phule Pune University , Pune , India.a Institute of Bioinformatics and Biotechnology , Savitribai Phule Pune University , Pune , India.a Institute of Bioinformatics and Biotechnology , Savitribai Phule Pune University , Pune , India.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

30052167

Citation

Tellis, Meenakshi B., et al. "Evolutionary and Structure-function Analysis Elucidates Diversification of Prokaryotic and Eukaryotic Trehalases." Journal of Biomolecular Structure & Dynamics, vol. 37, no. 11, 2019, pp. 2926-2937.
Tellis MB, Gujar NN, Joshi RS. Evolutionary and structure-function analysis elucidates diversification of prokaryotic and eukaryotic trehalases. J Biomol Struct Dyn. 2019;37(11):2926-2937.
Tellis, M. B., Gujar, N. N., & Joshi, R. S. (2019). Evolutionary and structure-function analysis elucidates diversification of prokaryotic and eukaryotic trehalases. Journal of Biomolecular Structure & Dynamics, 37(11), 2926-2937. https://doi.org/10.1080/07391102.2018.1497542
Tellis MB, Gujar NN, Joshi RS. Evolutionary and Structure-function Analysis Elucidates Diversification of Prokaryotic and Eukaryotic Trehalases. J Biomol Struct Dyn. 2019;37(11):2926-2937. PubMed PMID: 30052167.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Evolutionary and structure-function analysis elucidates diversification of prokaryotic and eukaryotic trehalases. AU - Tellis,Meenakshi B, AU - Gujar,Nidhi N, AU - Joshi,Rakesh S, Y1 - 2019/01/11/ PY - 2018/7/28/pubmed PY - 2020/7/2/medline PY - 2018/7/28/entrez KW - Evolution KW - domain architecture; structure; trehalase KW - glycosyl hydrolase KW - sugar metabolism SP - 2926 EP - 2937 JF - Journal of biomolecular structure & dynamics JO - J. Biomol. Struct. Dyn. VL - 37 IS - 11 N2 - Trehalase catalyses the breakdown of trehalose into two glucose moieties and is ubiquitous in all organisms. Here, we provide insights into the enigmatic origin and evolution of trehalase in major species. Study of taxonomic distribution, orthology, phylogeny and functional domains indicated that trehalase possibly originates from bacteria and was transmitted to other taxa through horizontal gene transfer. Domain analysis showed that glycosyl hydrolase family 37 is present in most of the sequences and represents dominant activity during evolution, and also, illustrating that cytosolic trehalase is primitive than its transmembrane form. Furthermore, it was observed that trehalase went through domain rearrangement to facilitate its activity in adverse environmental conditions like acidic pH. Gene context analysis depicts that trehalase neighbourhood consists of sugar transport and lipid metabolism genes. This highlights their relatedness in metabolic activity and similarity in gene regulation, respectively. Evolutionary and selection pressure analysis demonstrated that trehalase genes were duplicated and evolved under purifying selection, following horizontal gene transfer. Moreover, site-specific rate of evolution emphasized conservation of functionally important residues. In comparison with acid trehalase, neutral trehalase has an extra N-terminal extension. This study serves as an instigation to understand evolution and functionality of trehalase across diverse species. Communicated by Ramaswamy H. Sarma. SN - 1538-0254 UR - https://www.unboundmedicine.com/medline/citation/30052167/Evolutionary_and_structure_function_analysis_elucidates_diversification_of_prokaryotic_and_eukaryotic_trehalases_ L2 - http://www.tandfonline.com/doi/full/10.1080/07391102.2018.1497542 DB - PRIME DP - Unbound Medicine ER -