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Three amino acid substitutions contributing to thermostability of phosphoglucose isomerase in the Glanville fritillary butterfly.
Yang, Jianing; Wang, Di; Liu, Hui; Wang, Lin; Jin, Ling; Ahola, Virpi; Xu, Chongren; Wang, Rongjiang.
Afiliación
  • Yang J; School of Life Sciences, Peking University, Beijing, China.
  • Wang D; School of Life Sciences, Peking University, Beijing, China.
  • Liu H; School of Life Sciences, Peking University, Beijing, China.
  • Wang L; School of Life Sciences, Peking University, Beijing, China.
  • Jin L; School of Life Sciences, Peking University, Beijing, China.
  • Ahola V; Department of Biosciences, University of Helsinki, Helsinki, Finland.
  • Xu C; School of Life Sciences, Peking University, Beijing, China.
  • Wang R; School of Life Sciences, Peking University, Beijing, China.
Insect Sci ; 30(3): 758-770, 2023 Jun.
Article en En | MEDLINE | ID: mdl-36342954
ABSTRACT
Temperature is one of the most important environmental factors that affect organisms, especially ectotherms, due to its effects on protein stability. Understanding the general rules that govern thermostability changes in proteins to adapt high-temperature environments is crucial. Here, we report the amino acid substitutions of phosphoglucose isomerase (PGI) related to thermostability in the Glanville fritillary butterfly (Melitaea cinxia, Lepidoptera Nymphalidae). The PGI encoded by the most common allele in M. cinxia in the Chinese population (G3-PGI), which is more thermal tolerant, is more stable under heat stress than that in the Finnish population (D1-PGI). There are 5 amino acid substitutions between G3-PGI and D1-PGI. Site-directed mutagenesis revealed that the combination of amino acid substitutions of H35Q, M49T, and I64V may increase PGI thermostability. These substitutions alter the 3D structure to increase the interaction between 2 monomers of PGI. Through molecular dynamics simulations, it was found that the amino acid at site 421 is more stable in G3-PGI, confining the motion of the α-helix 420-441 and stabilizing the interaction between 2 PGI monomers. The strategy for high-temperature adaptation through these 3 amino acid substitutions is also adopted by other butterfly species (Boloria eunomia, Aglais urticae, Colias erate, and Polycaena lua) concurrent with M. cinxia in the Tianshan Mountains of China, i.e., convergent evolution in butterflies.
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Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Mariposas Diurnas / Fritillaria Límite: Animals Idioma: En Revista: Insect Sci Año: 2023 Tipo del documento: Article País de afiliación: China

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Mariposas Diurnas / Fritillaria Límite: Animals Idioma: En Revista: Insect Sci Año: 2023 Tipo del documento: Article País de afiliación: China