Molecular characterization and function of chitin deacetylase-like from the Chinese mitten crab, Eriocheir sinensis

被引:7
作者
Li, Xuguang [1 ,2 ]
Diao, Pengyun [1 ,2 ]
Chu, Jundong [1 ,2 ]
Zhou, Gang [1 ]
Zhou, Jun [1 ]
Lin, Hai [1 ]
Chen, Jianhua [2 ]
Zeng, Qingfei [3 ]
机构
[1] Freshwater Fisheries Res Inst Jiangsu Prov, Nanjing 210017, Peoples R China
[2] Jiangsu Ocean Univ, Jiangsu Key Lab Marine Biotechnol, Lianyungang 222005, Peoples R China
[3] Chinese Acad Sci, Nanjing Inst Geog & Limnol, State Key Lab Lake Sci & Environm, Nanjing 210008, Peoples R China
来源
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY | 2021年 / 256卷
基金
中国国家自然科学基金;
关键词
Chitin deacetylase; Chitin modification; Molting; RNA interference; Eriocheir sinensis; MOLT CYCLE; PROTEINS; ORGANIZATION; GASTROLITH; CUTICLE; OBSTRUCTOR; BINDING; FAMILY; GENE;
D O I
10.1016/j.cbpb.2021.110612
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Chitin deacetylases are essential enzymes in the chitin-modifying process and play vital roles in arthropod molting. In this study, we identified and characterized a chitin deacetylase-like (EsCDA-1) gene in the Chinese mitten crab, Eriocheir sinensis. The open reading frame of EsCDA-1 was 2555 bp and encoded 554 amino acid residues that contained typical domain structure of carbohydrate esterase family 4. Phylogenetic analysis reveal that EsCDA-1 belongs to the group I chitin deacetylase family. Quantitative real-time PCR analyses showed that EsCDA-1 was highly expressed in exoskeletal tissues and megalopa stages. During the molting cycle, EsCDA-1 was up-regulated periodically in the post-molt stage. Knockdown of EsCDA-1 resulted in the abnormal ultrastructure of cuticle, prevented molting to high mortality suggesting EsCDA-1 is indispensable for molting. The characterization and function analysis of the EsCDA-1 should provide useful reference for further research on the utility of key genes involved in the chitin metabolic pathway in the molting process of the Chinese mitten crab as well as other crustaceans.
引用
收藏
页数:9
相关论文
共 34 条
[1]   The search for proteins involved in the formation of crustacean cuticular structures [J].
Abehsera, Shai ;
Weil, Simy ;
Manor, Rivka ;
Sagi, Amir .
HYDROBIOLOGIA, 2018, 825 (01) :29-45
[2]   Analysis of functions of the chitin deacetylase gene family in Tribolium castaneum [J].
Arakane, Yasuyuki ;
Dixit, Radhika ;
Begum, Khurshida ;
Park, Yoonseong ;
Specht, Charles A. ;
Merzendorfer, Hans ;
Kramer, Karl J. ;
Muthukrishnan, Subbaratnam ;
Beeman, Richard W. .
INSECT BIOCHEMISTRY AND MOLECULAR BIOLOGY, 2009, 39 (5-6) :355-365
[3]   Structure and mechanism of chitin deacetylase from the fungal pathogen Colletotrichum lindemuthianum [J].
Blair, David E. ;
Hekmat, Omid ;
Schuttelkopf, Alexander W. ;
Shrestha, Binesh ;
Tokuyasu, Ken ;
Withers, Stephen G. ;
van Aalten, Daan M. F. .
BIOCHEMISTRY, 2006, 45 (31) :9416-9426
[4]   Domain organization and phylogenetic analysis of proteins from the chitin deacetylase gene family of Tribolium castaneum and three other species of insects [J].
Dixit, Radhika ;
Arakane, Yasuyuki ;
Specht, Charles A. ;
Richard, Chad ;
Kramer, Karl J. ;
Beeman, Richard W. ;
Muthukrishnan, Subbaratnam .
INSECT BIOCHEMISTRY AND MOLECULAR BIOLOGY, 2008, 38 (04) :440-451
[5]  
Fishery Bureau of Agriculture Ministry of China, 2020, CHIN FISH STAT YB, P34
[6]   Transcriptome analysis on the exoskeleton formation in early developmetal stages and reconstruction scenario in growth-moulting in Litopenaeus vannamei [J].
Gao, Yi ;
Wei, Jiankai ;
Yuan, Jianbo ;
Zhang, Xiaojun ;
Li, Fuhua ;
Xiang, Jianhai .
SCIENTIFIC REPORTS, 2017, 7
[7]   Proteomic analysis of the crayfish gastrolith chitinous extracellular matrix reveals putative protein complexes and a central role for GAP 65 [J].
Glazer, Lilah ;
Roth, Ziv ;
Weil, Simy ;
Aflalo, Eliahu D. ;
Khalaila, Isam ;
Sagi, Amir .
JOURNAL OF PROTEOMICS, 2015, 128 :333-343
[8]   A Protein Involved in the Assembly of an Extracellular Calcium Storage Matrix [J].
Glazer, Lilah ;
Shechter, Assaf ;
Tom, Moshe ;
Yudkovski, Yana ;
Weil, Simy ;
Aflalo, Eliahu David ;
Pamuru, Ramachandra Reddy ;
Khalaila, Isam ;
Bentov, Shmuel ;
Berman, Amir ;
Sagi, Amir .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2010, 285 (17) :12831-12839
[9]   Chitin Deacetylases: Structures, Specificities, and Biotech Applications [J].
Grifoll-Romero, Laia ;
Pascual, Sergi ;
Aragunde, Hugo ;
Biarnes, Xevi ;
Planas, Antoni .
POLYMERS, 2018, 10 (04)
[10]   A novel chitin-binding protein identified from the peritrophic membrane of the cabbage looper, Trichoplusia ni [J].
Guo, W ;
Li, GX ;
Pang, Y ;
Wang, P .
INSECT BIOCHEMISTRY AND MOLECULAR BIOLOGY, 2005, 35 (11) :1224-1234