Genome-Wide Analysis and Hormone Regulation of Chitin Deacetylases in Silkworm

Overview

Journal Int J Mol Sci

Publisher MDPI

Specialties Biochemistry
Chemistry
Molecular Biology

Date 2019 Apr 17

PMID 30987273

Citations 7

Authors

Ziyu Zhang

Jiamin Yan

Qing Liu

Yuhao Zhang

Jing Gong

Yong Hou

Affiliations

Soon will be listed here.

Abstract

Chitin deacetylases (CDAs) are a group of enzymes involved in chitin metabolism in insects; they play a critical role in molting, pupation, and the modification of chitin. In this study, we identified several CDAs in the silkworm, (CDA), and investigated the effect of various hormones on their expression in larvae and embryo cell lines (E). Eight genes encoding CDAs were identified in the silkworm genome. They showed different expression patterns in different tissues, and were classified into three types based on where they were expressed: the exoskeleton, digestive organs, and genital organs. Moreover, we found that some showed upregulated expression during the molting period, especially during the fourth molting period in larvae. We also verified that the expression of was upregulated by treatment with 20-hydroxyecdysone not only in larvae, but also in E cells. Interestingly, juvenile hormone analog treatment also upregulated the expression of some . The overexpression of several transcription factors revealed that the POU transcription factor POUM2 may play a major role in the regulation of expression. Finally, the silencing of and did not lead to abnormal phenotypes or death, but may have led to delays in silkworm pupation. These results provide important information about lepidopteran insects in terms of chitin deacetylases and the regulation of their expression.

Citing Articles

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References

Baker L, Specht C, Donlin M, Lodge J . Chitosan, the deacetylated form of chitin, is necessary for cell wall integrity in Cryptococcus neoformans. Eukaryot Cell. 2007; 6(5):855-67. PMC: 1899242. DOI: 10.1128/EC.00399-06. View

Wang S, Jayaram S, Hemphala J, Senti K, Tsarouhas V, Jin H . Septate-junction-dependent luminal deposition of chitin deacetylases restricts tube elongation in the Drosophila trachea. Curr Biol. 2006; 16(2):180-5. DOI: 10.1016/j.cub.2005.11.074. View

Toprak U, Baldwin D, Erlandson M, Gillott C, Hou X, Coutu C . A chitin deacetylase and putative insect intestinal lipases are components of the Mamestra configurata (Lepidoptera: Noctuidae) peritrophic matrix. Insect Mol Biol. 2008; 17(5):573-85. DOI: 10.1111/j.1365-2583.2008.00829.x. View

Cartharius K, Frech K, Grote K, Klocke B, Haltmeier M, Klingenhoff A . MatInspector and beyond: promoter analysis based on transcription factor binding sites. Bioinformatics. 2005; 21(13):2933-42. DOI: 10.1093/bioinformatics/bti473. View

Pearlmutter N, Lembi C . Localization of chitin in algal and fungal cell walls by light and electron microscopy. J Histochem Cytochem. 1978; 26(10):782-91. DOI: 10.1177/26.10.722047. View

Qu M, Ren Y, Liu Y, Yang Q . Studies on the chitin/chitosan binding properties of six cuticular proteins analogous to peritrophin 3 from Bombyx mori. Insect Mol Biol. 2017; 26(4):432-439. DOI: 10.1111/imb.12308. View

Tamura K, Stecher G, Peterson D, Filipski A, Kumar S . MEGA6: Molecular Evolutionary Genetics Analysis version 6.0. Mol Biol Evol. 2013; 30(12):2725-9. PMC: 3840312. DOI: 10.1093/molbev/mst197. View

Yu R, Liu W, Li D, Zhao X, Ding G, Zhang M . Helicoidal Organization of Chitin in the Cuticle of the Migratory Locust Requires the Function of the Chitin Deacetylase2 Enzyme (LmCDA2). J Biol Chem. 2016; 291(47):24352-24363. PMC: 5114393. DOI: 10.1074/jbc.M116.720581. View

Jindra M, Palli S, Riddiford L . The juvenile hormone signaling pathway in insect development. Annu Rev Entomol. 2012; 58:181-204. DOI: 10.1146/annurev-ento-120811-153700. View

10.

Dixit R, Arakane Y, Specht C, Richard C, Kramer K, Beeman R . Domain organization and phylogenetic analysis of proteins from the chitin deacetylase gene family of Tribolium castaneum and three other species of insects. Insect Biochem Mol Biol. 2008; 38(4):440-51. DOI: 10.1016/j.ibmb.2007.12.002. View

11.

Merzendorfer H, Zimoch L . Chitin metabolism in insects: structure, function and regulation of chitin synthases and chitinases. J Exp Biol. 2003; 206(Pt 24):4393-412. DOI: 10.1242/jeb.00709. View

12.

Daimon T, Katsuma S, Iwanaga M, Kang W, Shimada T . The BmChi-h gene, a bacterial-type chitinase gene of Bombyx mori, encodes a functional exochitinase that plays a role in the chitin degradation during the molting process. Insect Biochem Mol Biol. 2005; 35(10):1112-23. DOI: 10.1016/j.ibmb.2005.05.005. View

13.

Xi Y, Pan P, Ye Y, Yu B, Zhang C . Chitin deacetylase family genes in the brown planthopper, Nilaparvata lugens (Hemiptera: Delphacidae). Insect Mol Biol. 2014; 23(6):695-705. DOI: 10.1111/imb.12113. View

14.

Shi J, Mu L, Guo W, Li G . IDENTIFICATION AND HORMONE INDUCTION OF PUTATIVE CHITIN SYNTHASE GENES AND SPLICE VARIANTS IN Leptinotarsa decemlineata (SAY). Arch Insect Biochem Physiol. 2016; 92(4):242-58. DOI: 10.1002/arch.21331. View

15.

Yao Q, Zhang D, Tang B, Chen J, Chen J, Lu L . Identification of 20-hydroxyecdysone late-response genes in the chitin biosynthesis pathway. PLoS One. 2010; 5(11):e14058. PMC: 2987807. DOI: 10.1371/journal.pone.0014058. View

16.

Zhong X, Wang X, Tan X, Xia Q, Xiang Z, Zhao P . Identification and molecular characterization of a chitin deacetylase from Bombyx mori peritrophic membrane. Int J Mol Sci. 2014; 15(2):1946-61. PMC: 3958831. DOI: 10.3390/ijms15021946. View

17.

Guo W, Li G, Pang Y, Wang P . A novel chitin-binding protein identified from the peritrophic membrane of the cabbage looper, Trichoplusia ni. Insect Biochem Mol Biol. 2005; 35(11):1224-34. DOI: 10.1016/j.ibmb.2005.06.003. View

18.

Kaur S, Dhillon G . Recent trends in biological extraction of chitin from marine shell wastes: a review. Crit Rev Biotechnol. 2013; 35(1):44-61. DOI: 10.3109/07388551.2013.798256. View

19.

Marchler-Bauer A, Derbyshire M, Gonzales N, Lu S, Chitsaz F, Geer L . CDD: NCBI's conserved domain database. Nucleic Acids Res. 2014; 43(Database issue):D222-6. PMC: 4383992. DOI: 10.1093/nar/gku1221. View

20.

Araki Y, Ito E . A pathway of chitosan formation in Mucor rouxii. Enzymatic deacetylation of chitin. Eur J Biochem. 1975; 55(1):71-8. DOI: 10.1111/j.1432-1033.1975.tb02139.x. View