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Genome-wide identification and characterization of superoxide dismutases in four oyster species reveals functional differentiation in response to biotic and abiotic stress
被引:2
|作者:
Liu, Youli
[1
,2
,3
]
Bao, Zhenmin
[3
]
Lin, Zhihua
[1
,2
]
Xue, Qinggang
[1
,2
]
机构:
[1] Zhejiang Wanli Univ, Ninghai Inst Mariculture Breeding & Seed Ind, Ninghai 315604, Peoples R China
[2] Zhejiang Wanli Univ, Zhejiang Key Lab Aquat Germplasm Resource, Ningbo 315100, Peoples R China
[3] Ocean Univ China, Coll Marine Life Sci, Qingdao 266100, Peoples R China
基金:
中国国家自然科学基金;
关键词:
SOD family;
Genomic analysis;
Oysters;
Diversity;
OXIDATIVE STRESS;
LIFE-SPAN;
CU-ZN;
PROTEIN;
EVOLUTION;
CONSEQUENCES;
PREDICTION;
CLONING;
SOD;
D O I:
10.1186/s12864-022-08610-9
中图分类号:
Q81 [生物工程学(生物技术)];
Q93 [微生物学];
学科分类号:
071005 ;
0836 ;
090102 ;
100705 ;
摘要:
Background Oysters inhabit in the intertidal zone and may be suffered from environmental stresses, which can increase the production of reactive oxygen species (ROS), resulting in mass mortality. Superoxide dismutases (SODs) protect oysters from ROS damage through different mechanisms compared with vertebrates. However, the molecular and functional differentiation in oyster SODs were rarely analyzed. Result In this study, a total of 13, 13, 10, and 8 candidate SODs were identified in the genome of Crassostrea gigas, Crassostrea virginica, Crassostrea hongkongensis, and Saccostrea glomerata respectively. The domain composition, gene structure, subcellular locations, conserved ligands, and cis-elements elucidated the SODs into five groups (Mn-SODs, Cu-only-SODs, Cu/Zn ion ligand Cu/Zn-SOD with enzyme activity, Zn-only-SODs, and no ligand metal ions Cu/Zn-SODs). For single domain Cu/Zn-SODs, only one cytosolic Cu/Zn-SOD (cg_XM_034479061.1) may conserve enzymatic activity while most extracellular Cu/Zn-SOD proteins appeared to lose SOD enzyme activity according to conserved ligand amino acid analysis and expression pattern under biotic and abiotic stress in C. gigas. Further, multi-domain-SODs were identified and some of them were expressed in response to biotic and abiotic stressors in C. gigas. Moreover, the expression patterns of these genes varied in response to different stressors, which may be due to the cis-elements in the gene promoter. Conclusion These findings revealed the most extracellular Cu/Zn-SOD proteins appeared to lose SOD enzyme activity in oysters. Further, our study revealed that only one cytosolic Cu/Zn-SOD (cg_XM_034479061.1) may conserve enzymatic activity of SOD. Moreover, the expression patterns of these genes varied in response to different stressors, which may be due to the cis-elements in the promoter. This study provides important insights into the mechanisms through which oysters adapt to harsh intertidal conditions, as well as potential biomarkers of stress response in related species.
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