1. Academic Validation
  2. The acetylation modification regulates the stability of Bm30K-15 protein and its mechanism in silkworm, Bombyx mori

The acetylation modification regulates the stability of Bm30K-15 protein and its mechanism in silkworm, Bombyx mori

  • Arch Insect Biochem Physiol. 2021 Jul;107(3):e21823. doi: 10.1002/arch.21823.
Jiao Lv 1 Shouliang Li 1 Yue Liu 2 Zihan Sun 1 Dan Wang 1 Zhengying You 1 Caiying Jiang 1 Qing Sheng 1 Zuoming Nie 1
Affiliations

Affiliations

  • 1 College of Life Sciences and Medicine, Zhejiang Sci-Tech University, Hangzhou, China.
  • 2 Zhejiang Institute of Economics and Trade, Hangzhou, China.
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.

Keywords

Bm30K-15; acetylation; protein stability; ubiquitination.

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