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Int J Mol Sci
2019 Sep 09;2018:. doi: 10.3390/ijms20184423.
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Lysine Acetylation is an Important Post-Translational Modification that Modulates Heat Shock Response in the Sea Cucumber Apostichopus japonicus.
Xu D
,
Wang X
.
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Heat stress (HS) is an important factor for the survival of the marine organism Apostichopus japonicus. Lysine acetylation is a pivotal post-translational modification that modulates diverse physiological processes including heat shock response (HSR). In this study, 4028 lysine acetylation sites in 1439 proteins were identified in A. japonicus by acetylproteome sequencing. A total of 13 motifs were characterized around the acetylated lysine sites. Gene Ontology analysis showed that major acetylated protein groups were involved in "oxidation-reduction process", "ribosome", and "protein binding" terms. Compared to the control group, the acetylation quantitation of 25 and 41 lysine sites changed after 6 and 48 h HS. Notably, lysine acetyltransferase CREB-binding protein (CBP) was identified to have differential acetylation quantitation at multiple lysine sites under HS. Various chaperones, such as caseinolytic peptidase B protein homolog (CLBP), T-complex protein 1 (TCP1), and cyclophilin A (CYP1), showed differential acetylation quantitation after 48 h HS. Additionally, many translation-associated proteins, such as ribosomal proteins, translation initiation factor (IF), and elongation factors (EFs), had differential acetylation quantitation under HS. These proteins represented specific interaction networks. Collectively, our results offer novel insight into the complex HSR in A. japonicus and provide a resource for further mechanistic studies examining the regulation of protein function by lysine acetylation.
41706175 National Natural Science Foundation of China, 31702355 National Natural Science Foundation of China, OF2018NO03 Qingdao National Laboratory for Marine Science and Technology, 20173B03 Qingdao National Laboratory for Marine Science and Technology, KLMEES201804 Institute of Oceanology, Chinese Academy of Sciences, ZR2017BD007 Natural Science Foundation of Shandong Province
Figure 1. Proteome-wide identification of lysine acetylation sites in sea cucumbers. (A) Experimental strategy for quantifying lysine acetylation. (B) Peptide number and peptide length. (C) Number of proteins and number of modified sites.
Figure 2. Properties of lysine acetylation sites. (A) A total of 13 enriched motifs and the number of according peptides. (B) Sequences of the top five motifs with the biggest probability. (C) Sequence probability logos of significantly enriched acetylation site motifs for ±7 amino acids around the lysine acetylation sites.
Figure 3. Functional classification of acetylated proteins identified in sea cucumbers. (A) Classification of acetylated proteins based on the Gene Ontology (GO) database. (B) Classification of acetylated proteins based on the Clusters of Orthologous Groups (COG) database.
Figure 5. Interaction networks of the proteins with differential numbers of acetylated sites. (A) The major interaction network of the proteins with differential numbers of acetylated sites. (B) Five proteins pairs with interactions. The color of the circles depends on the functions of the proteins. The width of the lines is positively correlated with the strength of interaction.
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