College of Life Sciences and Medicine, Zhejiang Sci-Tech University, Hangzhou, China.
Zhejiang Institute of Economics and Trade, Hangzhou, China.
Arch Insect Biochem Physiol. 2021 Jul;107(3):e21823. doi: 10.1002/arch.21823. Epub 2021 Jun 1.
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.
30K 蛋白是主要的家蚕血液蛋白，参与多种生理过程，如营养和能量储存、胚胎发生、免疫反应和抑制细胞凋亡。Bm30K-15 蛋白是 30K 蛋白之一，在家蚕五龄幼虫的血液中含量丰富。我们之前发现 Bm30K-15 蛋白可以被乙酰化。在本研究中，我们发现乙酰化可以提高 Bm30K-15 的蛋白质稳定性。进一步的探索证实，乙酰化引起的蛋白质稳定性增加是由于乙酰化和泛素化之间的竞争。总之，这些发现旨在深入了解乙酰化修饰对 Bm30K-15 蛋白水平和稳定性的影响，以及其在家蚕 Bombyx mori 中存在的可能分子机制。
