title: Lysine acetylation stabilizes SP2 protein in the silkworm Bombyx mori.
abstract: Lysine acetylation (Kac) is a vital post-translational modification that plays an important role in many cellular processes in organisms. In the present study, the nutrient storage proteins in hemolymph were first found to be highly acetylated-particularly SP2 protein, which contains 20 potential Kac sites. Further results confirmed that lysine acetylation could stabilize and up-regulate the protein level of anti-apoptosis protein SP2, thereby improving the survival of H2O2-treated BmN cells and suppressing the apoptosis induced by H2O2. The potential mechanism involved in the inhibition of ubiquitin-mediated proteasomal degradation by crosstalk between lysine acetylation and ubiquitination. Our results showed that the increase in the acetylation level by TSA could decrease the ubiquitination and improve the protein level of SP2, indicating that lysine acetylation could influence the SP2 protein level through competition between ubiquitination and the suppression of ubiquitin-mediated proteasomal degradation, thereby stabilizing the protein. SP2 is a major nutrient storage protein from hemolymph for amino acid storage and utilization. The crosstalk between lysine acetylation and ubiquitination of SP2 might imply an important role of lysine acetylation for nutrient storage and utilization in silkworm.
authors.affiliation: College of Life Sciences, Zhejiang Sci-Tech University, Hangzhou 310018, China.
authors.forename: Yong
authors.initials: Y
authors.lastname: Zhou
authors.affiliation: College of Life Sciences, Zhejiang Sci-Tech University, Hangzhou 310018, China.
authors.forename: Chengcheng
authors.initials: C
authors.lastname: Wu
authors.affiliation: College of Life Sciences, Zhejiang Sci-Tech University, Hangzhou 310018, China.
authors.forename: Qing
authors.initials: Q
authors.lastname: Sheng
authors.affiliation: College of Life Sciences, Zhejiang Sci-Tech University, Hangzhou 310018, China.
authors.forename: Caiying
authors.initials: C
authors.lastname: Jiang
authors.affiliation: College of Life Sciences, Zhejiang Sci-Tech University, Hangzhou 310018, China.
authors.forename: Qin
authors.initials: Q
authors.lastname: Chen
authors.affiliation: College of Life Sciences, Zhejiang Sci-Tech University, Hangzhou 310018, China.
authors.forename: Zhengbing
authors.initials: Z
authors.lastname: Lv
authors.affiliation: College of Materials and Textile, Zhejiang Sci-Tech University, Hangzhou 310018, China.
authors.forename: Juming
authors.initials: J
authors.lastname: Yao
authors.affiliation: College of Life Sciences, Zhejiang Sci-Tech University, Hangzhou 310018, China; College of Materials and Textile, Zhejiang Sci-Tech University, Hangzhou 310018, China. Electronic address: wuxinzm@126.com.
authors.forename: Zuoming
authors.initials: Z
authors.lastname: Nie
mesh_terms: D000107:Acetylation; D000818:Animals; D015153:Blotting, Western; D012831:Bombyx / Q000254:growth & development / Q000378:metabolism*; D002851:Chromatography, High Pressure Liquid; D019476:Insect Proteins / Q000378:metabolism*; D007814:Larva / Q000254:growth & development / Q000378:metabolism; D008239:Lysine / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D053719:Tandem Mass Spectrometry
chemical_list: D019476:Insect Proteins; C041137:storage proteins, Insecta; D008239:Lysine
keywords: Crosstalk; Lysine acetylation; Nutrient storage and utilization; SP2; Ubiquitination