生物
乙酰化
非生物成分
非生物胁迫
细胞生物学
生物化学
遗传学
作者
Xiaodi Gong,Yaqian Huang,Yan Liang,Yundong Yuan,Yuhao Liu,Tongwen Han,Shujia Li,Hengbin Gao,Bo Lv,Xiahe Huang,Eric Linster,Yingchun Wang,Markus Wirtz,Yonghong Wang
标识
DOI:10.1016/j.molp.2022.03.001
摘要
N-terminal acetylation is one of the most common protein modifications in eukaryotes, and approximately 40% of human and plant proteomes are acetylated by ribosome-associated N-terminal acetyltransferase A (NatA) in a co-translational manner. However, the in vivo regulatory mechanism of NatA and the global impact of NatA-mediated N-terminal acetylation on protein fate remain unclear. Here, we identify Huntingtin Yeast partner K (HYPK), an evolutionarily conserved chaperone-like protein, as a positive regulator of NatA activity in rice. We found that loss of OsHYPK function leads to developmental defects in rice plant architecture but increased resistance to abiotic stresses, attributable to perturbation of the N-terminal acetylome and accelerated global protein turnover. Furthermore, we demonstrated that OsHYPK is also a substrate of NatA and that N-terminal acetylation of OsHYPK promotes its own degradation, probably through the Ac/N-degron pathway, which could be induced by abiotic stresses. Taken together, our findings suggest that the OsHYPK-NatA complex plays a critical role in coordinating plant development and stress responses by dynamically regulating NatA-mediated N-terminal acetylation and global protein turnover, which are essential for maintaining adaptive phenotypic plasticity in rice.
科研通智能强力驱动
Strongly Powered by AbleSci AI