Chen Yanmei, Lv Jiao, Zu Guowei, Yang Fan, Geng Jiasheng, You Zhengying, Jiang Caiying, Sheng Qing, Nie Zuoming
Zhejiang Provincial Key Laboratory of Silkworm Bioreactor and Biomedicine, College of Life Sciences and Medicine, Zhejiang Sci-Tech University, Hangzhou 310018, China.
Insects. 2023 Mar 23;14(4):309. doi: 10.3390/insects14040309.
Acetylation is an important and reversible post-translational modification (PTM) of protein, which is involved in many cellular physiological processes. In previous studies, lots of nutrient storage proteins were found to be highly acetylated in silkworms, and acetylation can improve the stability of these proteins. However, the related acetyltransferase was not involved. In the present work, a nutrient storage protein, apolipophorin II (BmApoLp-II), was further confirmed to be acetylated, and the acetylation could improve its protein expression. Furthermore, RNAi and Co-IP showed that the acetyltransferase BmCBP was found to catalyze the acetylation modification of BmApoLp-II, and thus affect its protein expression. Meanwhile, it was proved that acetylation could improve the stability of the BmApoLp-II protein by completing its ubiquitination. These results lay a foundation for further study on the mechanism of regulating nutrition storage and hydrolysis utilization of storage proteins by BmCBP and the acetylation in the silkworm .
乙酰化是蛋白质重要的可逆性翻译后修饰（PTM），参与许多细胞生理过程。在以往研究中，发现家蚕中许多营养储存蛋白高度乙酰化，且乙酰化可提高这些蛋白的稳定性。然而，相关乙酰转移酶并未涉及。在本研究中，一种营养储存蛋白，载脂蛋白II（BmApoLp-II），被进一步证实发生乙酰化，且乙酰化可提高其蛋白表达。此外，RNA干扰和免疫共沉淀表明，发现乙酰转移酶BmCBP催化BmApoLp-II的乙酰化修饰，从而影响其蛋白表达。同时，证明乙酰化可通过完成其泛素化来提高BmApoLp-II蛋白的稳定性。这些结果为进一步研究BmCBP调控储存蛋白营养储存及水解利用机制以及家蚕中的乙酰化奠定了基础。
