Cho Seok Keun, Ryu Moon Young, Shah Pratik, Poulsen Christian Peter, Yang Seong Wook
Department of Systems Biology, College of Life Science and Biotechnology, Yonsei University 03722, Korea.
Department of Biomedical Engineering, University of California Irvine, 92697, CA, USA.
Mol Cells. 2016 Aug 31;39(8):581-6. doi: 10.14348/molcells.2016.0085. Epub 2016 Jul 20.
Post-translational modifications (PTMs) of proteins are essential to increase the functional diversity of the proteome. By adding chemical groups to proteins, or degrading entire proteins by phosphorylation, glycosylation, ubiquitination, neddylation, acetylation, lipidation, and proteolysis, the complexity of the proteome increases, and this then influences most biological processes. Although small RNAs are crucial regulatory elements for gene expression in most eukaryotes, PTMs of small RNA microprocessor and RNA silencing components have not been extensively investigated in plants. To date, several studies have shown that the proteolytic regulation of AGOs is important for host-pathogen interactions. DRB4 is regulated by the ubiquitin-proteasome system, and the degradation of HYL1 is modulated by a de-etiolation repressor, COP1, and an unknown cytoplasmic protease. Here, we discuss current findings on the PTMs of microprocessor and RNA silencing components in plants.
蛋白质的翻译后修饰（PTMs）对于增加蛋白质组的功能多样性至关重要。通过给蛋白质添加化学基团，或通过磷酸化、糖基化、泛素化、类泛素化、乙酰化、脂化和蛋白水解作用降解整个蛋白质，蛋白质组的复杂性增加，进而影响大多数生物过程。尽管小RNA是大多数真核生物中基因表达的关键调控元件，但小RNA微处理器和RNA沉默组件的翻译后修饰在植物中尚未得到广泛研究。迄今为止，多项研究表明AGO的蛋白水解调控对于宿主-病原体相互作用很重要。DRB4受泛素-蛋白酶体系统调控，而HYL1的降解则由去黄化抑制因子COP1和一种未知的细胞质蛋白酶调节。在此，我们讨论植物中微处理器和RNA沉默组件翻译后修饰的当前研究结果。
