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The acetylation modification regulates the stability of Bm30K‐15 protein and its mechanism in silkworm, Bombyx mori
Author(s) -
Lv Jiao,
Li Shouliang,
Liu Yue,
Sun Zihan,
Wang Dan,
You Zhengying,
Jiang Caiying,
Sheng Qing,
Nie Zuoming
Publication year - 2021
Publication title -
archives of insect biochemistry and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.576
H-Index - 66
eISSN - 1520-6327
pISSN - 0739-4462
DOI - 10.1002/arch.21823
Subject(s) - bombyx mori , hemolymph , acetylation , biology , ubiquitin , biochemistry , bombyx , lysine , bombycidae , microbiology and biotechnology , amino acid , gene
Abstract The 30 K proteins are the major silkworm hemolymph proteins and are involved in a variety of physiological processes, such as nutrient and energy storage, embryogenesis, immune response, and inhibition of apoptosis. The Bm30K‐15 protein is one of the 30 K proteins and is abundant in the hemolymph of fifth instar silkworm larva. We previously found that the Bm30K‐15 protein can be acetylated. In the present study, we found that acetylation can improve the protein stability of Bm30K‐15. Further exploration confirmed that the increase in protein stability by acetylation was caused by competition between acetylation and ubiquitination. In summary, these findings aim to provide insight into the effect of acetylation modification on the protein level and stability of the Bm30K‐15 and the possible molecular mechanism of its existence in silkworm, Bombyx mori .