title: Global proteomic analysis of protein acetylation affecting metabolic regulation in Daphnia pulex.
abstract: Daphnia (Daphnia pulex) is a small planktonic crustacean and a key constituent of aquatic ecosystems. It is generally used as a model organism to study environmental toxic problems. In the past decade, genomic and proteomic datasets of Daphnia have been developed. The proteomic dataset allows for the investigation of toxicological effects in the context of "Daphnia proteomics," resulting in greater insights for toxicological research. To exploit Daphnia for ecotoxicological research, information on the post-translational modification (PTM) of proteins is necessary, as this is a critical regulator of biological processes. Acetylation of lysine (Kac) is a reversible and highly regulated PTM that is associated with diverse biological functions. However, a comprehensive description of Kac in Daphnia is not yet available. To understand the cellular distribution of lysine acetylation in Daphnia, we identified 98 acetylation sites in 65 proteins by immunoprecipitation using an anti-acetyllysine antibody and a liquid chromatography system supported by mass spectroscopy. We identified 28 acetylated sites related to metabolic proteins and six acetylated enzymes associated with the TCA cycle in Daphnia. From GO and KEGG enrichment analyses, we showed that Kac in D. pulex is highly enriched in proteins associated with metabolic processes. Our data provide the first global analysis of Kac in D. pulex and is an important resource for the functional analysis of Kac in this organism.
authors.affiliation: College of Pharmacy, Research Institute of Pharmaceutical Sciences, Kyungpook National University, Daegu 41566, South Korea.
authors.forename: Oh Kwang
authors.initials: OK
authors.lastname: Kwon
authors.affiliation: College of Pharmacy, Research Institute of Pharmaceutical Sciences, Kyungpook National University, Daegu 41566, South Korea.
authors.forename: Juhee
authors.initials: J
authors.lastname: Sim
authors.affiliation: College of Pharmacy, Research Institute of Pharmaceutical Sciences, Kyungpook National University, Daegu 41566, South Korea.
authors.forename: Sun Ju
authors.initials: SJ
authors.lastname: Kim
authors.affiliation: College of Pharmacy, Yeungnam University, Gyeongsan 38541, South Korea.
authors.forename: Hye Ryeung
authors.initials: HR
authors.lastname: Oh
authors.affiliation: College of Pharmacy, Yeungnam University, Gyeongsan 38541, South Korea.
authors.forename: Doo Hyun
authors.initials: DH
authors.lastname: Nam
authors.affiliation: College of Pharmacy, Research Institute of Pharmaceutical Sciences, Kyungpook National University, Daegu 41566, South Korea. Electronic address: sangkyu@knu.ac.kr.
authors.forename: Sangkyu
authors.initials: S
authors.lastname: Lee
mesh_terms: D000107:Acetylation; D000818:Animals; D003621:Daphnia / Q000378:metabolism*; D004734:Energy Metabolism / Q000235:genetics; D011506:Proteins / Q000378:metabolism; D040901:Proteomics
chemical_list: D011506:Proteins
keywords: Daphnia pulex; Lysine acetylation; Post-translational modification; Proteomics