351. Comparative proteomic analysis of Aurelia coerulea for its locomotion system molecular structure-function inference.
- Author
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Ge, Mengxiao, Liu, Wenwen, Ma, Chaoqun, Yan, Zhenpeng, Liang, Hongyu, Xu, Zheng, Mariottini, Gian Luigi, Zhang, Jing, Zhao, Xianxian, Yang, Yi, and Xiao, Liang
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CONTRACTILE proteins , *MOLECULAR weights , *AMINO acid sequence , *CONVERGENT evolution , *GENE regulatory networks , *COMPARATIVE studies , *PROTEOMICS - Abstract
Rhythmic contraction and autonomous movement play a key role in the predation, production and displacement of jellyfish. Four independent body parts of the jellyfish Aurelia coerulea , including Bell, Tentacle, Oral arm and Gastric pouch were extracted and have been carried out a compared proteomics by liquid chromatography-mass spectrometry/mass-spectrometry (LC-MS/MS). ResultsA total of 13,429 peptides and 1916 proteins with molecular weights in the range of 10.6–980.9 kDa were identified, where 1916, 1562, 1474 and 1441 proteins were matched in the Gastric pouch, Tentacle, Oral arm and Bell, respectively. Gene Ontology (GO) analysis showed that translation, cytoplasma and ATP binding occupy the top differential terms of the three subdomains Biological process, Cellular Component and Molecular Function. A total of 326 pathways were successfully mapped that are mainly associated with intracellular synthesis, metabolism as well as intracellular functions. Moreover, a total of 27 contractile machinery associated proteins including 22 myosin, 3 actin and 2 tropomyosin were identified. Our results provide a composition profile in the four independent body parts of the jellyfish A. coerulea , of which the identified muscular proteins will greatly help in the understanding of the structural and functional relationship, as well as their operating mechanisms in the jellyfish locomotion system. Omics studies have gained a new overall insight into the function of gene and protein networks during the development of motor systems in both bilateral and radial symmetrical animals. A compared proteomics using the label-free method of nano-LC-MS/MS has been performed through the four independent body parts of the moon jellyfish A. coerulea , including Bell, Tentacle, Oral arm and Gastric pouch. In addition to conventional bioinformatics analyses such as GO and KEGG, we have scanned the locomotion-related components, aligned their sequences, simulated three dimensional structures as well as did the molecular phylogenetic analyses. Our investigation provides a composition profile in the four independent body parts of the jellyfish A. coerulea , of which the identified muscular proteins will greatly help in the understanding of the structural and functional relationship, as well as their operating mechanisms in the jellyfish locomotion system. A total of 1916 proteins were identified, where 1916, 1562, 1474 and 1441 proteins were matched in the Gastric pouch, Tentacle, Oral arm and Bell, respectively through a compared proteomics by nano-LC-MS/MS.Proteomic indexes, including amino acids (AAs) distribution, molecular weight (MW) distribution and electric point distribution, peptide count distribution, protein sequence coverage and exponentially modified protein abundance index (emPAI) distribution indicate the relationship of proteins from the four different body parts of Aurelia coerulea. Unlabelled Image • A total of 27 contractile machinery associated proteins including 22 myosin, 3 actin and 2 tropomyosin were identified, indicating a convergent evolution of muscular molecules from the jellyfish to the bilaterians. • A total of 1273 overlapped proteins out of 1916 overall identified proteins were analyzed from the four different body parts of the jellyfish A. coerulea , indicating a low difference of protein composition among the four body parts. • We have scanned the locomotion-related components, aligned their sequences, simulated three dimensional structures as well as done the molecular phylogenetic analyses as an important reference for the structure-function relationship of the muscular molecules. [ABSTRACT FROM AUTHOR]
- Published
- 2019
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