Structural and functional analysis of aquaporins in Bombus terrestris.

Autor: Ma X; Jilin Provincial Key Laboratory of Animal Resource Conservation and Utilization, Northeast Normal University, Changchun, Jilin 116000, People's Republic of China; Key Laboratory of Vegetation Ecology, MOE, Northeast Normal University, Changchun, Jilin 116000, People's Republic of China., Chang X; Jilin Provincial Key Laboratory of Animal Resource Conservation and Utilization, Northeast Normal University, Changchun, Jilin 116000, People's Republic of China; Key Laboratory of Vegetation Ecology, MOE, Northeast Normal University, Changchun, Jilin 116000, People's Republic of China., Liu G; Jilin Provincial Key Laboratory of Animal Resource Conservation and Utilization, Northeast Normal University, Changchun, Jilin 116000, People's Republic of China; Key Laboratory of Vegetation Ecology, MOE, Northeast Normal University, Changchun, Jilin 116000, People's Republic of China., Han Q; Innovation Center of Pesticide Research, Department of Applied Chemistry, College of Science, China Agricultural University, Beijing 100193, People's Republic of China., Ke H; Jilin Provincial Key Laboratory of Animal Resource Conservation and Utilization, Northeast Normal University, Changchun, Jilin 116000, People's Republic of China; Key Laboratory of Vegetation Ecology, MOE, Northeast Normal University, Changchun, Jilin 116000, People's Republic of China., Ren B; Jilin Provincial Key Laboratory of Animal Resource Conservation and Utilization, Northeast Normal University, Changchun, Jilin 116000, People's Republic of China; Key Laboratory of Vegetation Ecology, MOE, Northeast Normal University, Changchun, Jilin 116000, People's Republic of China., Wang Y; Jilin Provincial Key Laboratory of Animal Resource Conservation and Utilization, Northeast Normal University, Changchun, Jilin 116000, People's Republic of China; Key Laboratory of Vegetation Ecology, MOE, Northeast Normal University, Changchun, Jilin 116000, People's Republic of China. Electronic address: wangyl392@nenu.edu.cn.
Jazyk: angličtina
Zdroj: International journal of biological macromolecules [Int J Biol Macromol] 2024 Aug; Vol. 275 (Pt 2), pp. 133692. Date of Electronic Publication: 2024 Jul 06.
DOI: 10.1016/j.ijbiomac.2024.133692
Abstrakt: Bombus terrestris are efficient pollinators in forestry and agriculture, with higher cold tolerance than other bees. Yet, their cold tolerance mechanism remains unclear. Aquaporins (AQPs) function as cell membrane proteins facilitating rapid water flow, aiding in osmoregulation. Recent studies highlight the importance of insect AQPs in dehydration and cold stress. Comparative transcriptome analysis of B. terrestris under cold stress revealed up-regulation of four AQPs, indicating their potential role in cold tolerance. Seven AQPs-Eglp1, Eglp2, Eglp3, DRIP, PRIP, Bib, and AQP12L-have been identified in B. terrestris. These are widely expressed in various tissues, particularly in the alimentary canal and Malpighian tubules. Functional analysis of BterAQPs in the Xenopus laevis oocytes expressing system showed distinct water and glycerol selectivity, with BterDrip exhibiting the highest water permeability. Molecular modeling of BterDrip revealed six transmembrane domains, two NPA motifs, and an ar/R constriction region (Phe131, His256, Ser265, and Arg271), likely contributing to its water selectivity. Silencing BterDRIP accelerated mortality in B. terrestris under cold stress, highlighting the crucial role of BterDRIP in their cold tolerance and providing a molecular mechanism for their cold adaptation.
Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
(Copyright © 2024 Elsevier B.V. All rights reserved.)
Databáze: MEDLINE
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