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Molecular evolutionary mechanisms driving functional diversification of α-glucosidase in Lepidoptera.
Sci Rep. 2017 04 12; 7:45787.SR

Abstract

The digestive tract of lepidopteran insects is unique given its highly alkaline pH. The adaptive plasticity of digestive enzymes in this environment is crucial to the highly-efficient nutritional absorption in Lepidoptera. However, little is known about the molecular adaptation of digestive enzymes to this environment. Here, we show that lepidopteran α-glucosidase, a pivotal digestive enzyme, diverged into sucrose hydrolase (SUH) and other maltase subfamilies. SUH, which is specific for sucrose, was only detected in Lepidoptera. It suggests that lepidopteran insects have evolved an enhanced ability to hydrolyse sucrose, their major energy source. Gene duplications and exon-shuffling produced multiple copies of α-glucosidase in different microsyntenic regions. Furthermore, SUH showed significant functional divergence (FD) compared with maltase, which was affected by positive selection at specific lineages and codons. Nine sites, which were involved in both FD and positive selection, were located around the ligand-binding groove of SUH. These sites could be responsible for the ligand-binding preference and hydrolytic specificity of SUH for sucrose, and contribute to its conformational stability. Overall, our study demonstrated that positive selection is an important evolutionary force for the adaptive diversification of α-glucosidase, and for the exclusive presence of membrane-associated SUHs in the unique lepidopteran digestive tract.

Authors+Show Affiliations

College of Animal Sciences, Zhejiang University, Hangzhou 310058, China.College of Animal Sciences, Zhejiang University, Hangzhou 310058, China.College of Animal Sciences, Zhejiang University, Hangzhou 310058, China.College of Animal Sciences, Zhejiang University, Hangzhou 310058, China.College of Animal Sciences, Zhejiang University, Hangzhou 310058, China.College of Animal Sciences, Zhejiang University, Hangzhou 310058, China.College of Animal Sciences, Zhejiang University, Hangzhou 310058, China.College of Animal Sciences, Zhejiang University, Hangzhou 310058, China.

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

28401928

Citation

Li, Xiaotong, et al. "Molecular Evolutionary Mechanisms Driving Functional Diversification of Α-glucosidase in Lepidoptera." Scientific Reports, vol. 7, 2017, p. 45787.
Li X, Shi L, Zhou Y, et al. Molecular evolutionary mechanisms driving functional diversification of α-glucosidase in Lepidoptera. Sci Rep. 2017;7:45787.
Li, X., Shi, L., Zhou, Y., Xie, H., Dai, X., Li, R., Chen, Y., & Wang, H. (2017). Molecular evolutionary mechanisms driving functional diversification of α-glucosidase in Lepidoptera. Scientific Reports, 7, 45787. https://doi.org/10.1038/srep45787
Li X, et al. Molecular Evolutionary Mechanisms Driving Functional Diversification of Α-glucosidase in Lepidoptera. Sci Rep. 2017 04 12;7:45787. PubMed PMID: 28401928.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Molecular evolutionary mechanisms driving functional diversification of α-glucosidase in Lepidoptera. AU - Li,Xiaotong, AU - Shi,Liangen, AU - Zhou,Yanyan, AU - Xie,Hongqing, AU - Dai,Xiangping, AU - Li,Rongqiao, AU - Chen,Yuyin, AU - Wang,Huabing, Y1 - 2017/04/12/ PY - 2016/12/05/received PY - 2017/03/01/accepted PY - 2017/4/13/entrez PY - 2017/4/13/pubmed PY - 2018/11/18/medline SP - 45787 EP - 45787 JF - Scientific reports JO - Sci Rep VL - 7 N2 - The digestive tract of lepidopteran insects is unique given its highly alkaline pH. The adaptive plasticity of digestive enzymes in this environment is crucial to the highly-efficient nutritional absorption in Lepidoptera. However, little is known about the molecular adaptation of digestive enzymes to this environment. Here, we show that lepidopteran α-glucosidase, a pivotal digestive enzyme, diverged into sucrose hydrolase (SUH) and other maltase subfamilies. SUH, which is specific for sucrose, was only detected in Lepidoptera. It suggests that lepidopteran insects have evolved an enhanced ability to hydrolyse sucrose, their major energy source. Gene duplications and exon-shuffling produced multiple copies of α-glucosidase in different microsyntenic regions. Furthermore, SUH showed significant functional divergence (FD) compared with maltase, which was affected by positive selection at specific lineages and codons. Nine sites, which were involved in both FD and positive selection, were located around the ligand-binding groove of SUH. These sites could be responsible for the ligand-binding preference and hydrolytic specificity of SUH for sucrose, and contribute to its conformational stability. Overall, our study demonstrated that positive selection is an important evolutionary force for the adaptive diversification of α-glucosidase, and for the exclusive presence of membrane-associated SUHs in the unique lepidopteran digestive tract. SN - 2045-2322 UR - https://www.unboundmedicine.com/medline/citation/28401928/Molecular_evolutionary_mechanisms_driving_functional_diversification_of_α_glucosidase_in_Lepidoptera_ L2 - http://dx.doi.org/10.1038/srep45787 DB - PRIME DP - Unbound Medicine ER -