Molecular characteristics and gene expression of the Cnaphalocrocis medinalis (Guenée) ABCG3 transporter protein
Author of the article:Lü Ke;HE Xiao-Chan;XU Hong-Xing;Lü Zhong-Xian;YANG Ya-Jun
Author's Workplace:State Key Laboratory Breeding Base for Zhejiang Sustainable Pest and Disease Control; Key Laboratory of Biotechnology in Plant Protection, Ministry of Agriculture and Rural Affairs; Institute of Plant Protection and Microbiology, Zhejiang Academy of Agricultural Sciences, Hangzhou 310021, China; College of Plant Protection, Nanjing Agricultural University, Nanjing 210095, China; Jinhua Academy of Agricultural Sciences, Jinhua 321000, China
Key Words:Cnaphalocrocis medinalis (Guenée); ABCG transporter; protein structure; expression analysis
Abstract:
[Objectives] To improve understanding of the
characteristics and expression profile of the Cnaphalocrocis medinalis ABCG3 protein, one of
the ATP-binding cassette transporter (ABC transporter) transmembrane proteins
found in many organisms that is involved in the transport of nutrients and
exogenous toxins. [Methods] We used bioinformatics to
investigate the molecular properties of the C. medinalis ABCG3
transporter protein, and RT-qPCR to determine its expression patterns in
different larval instars and tissues. [Results] C. medinalis ABCG3 is a
half-transporter protein with 1 055 amino acids, a molecular weight of 118.95
ku and an isoelectric point of 8.78. It has a transmembrane domain (TMD) and a nucleic
acid binding domain (NBD). The protein is predicted to be located in the
endoplasmic reticulum, and has a 43.51% α-helix, a 7.01% β-angle, a 18.29%
lamellae and a 31.18% irregular roll. A phylogenetic tree of C. medinalis ABCG3 and that of five other lepidopteran species suggests that C. medinalis ABCG3 is most closely related to that of the monarch butterfly (Danaus
plexippus). The ABCG3 gene was found to be expressed in all larval
instars and tissues that were investigated. Expression was higher in fifth
instar larvae than in other instars, and higher in the hemolymph and fat body than
in other tissues. [Conclusion] These
findings clarify the structural properties and expression patterns of the ABC
transporter family in C. medinalis, and thereby provide a platform for further
investigation of the function of ABC transporters in this species.