The Fng3 ING protein regulates H3 acetylation and H4 deacetylation by interacting with two distinct histone‐modifying complexes
The Fng3 ING protein regulates H3 acetylation and H4 deacetylation by interacting with two distinct histone‐modifying complexes
复制标题
Fng3 ING 蛋白通过与两种不同的组蛋白修饰复合物相互作用来调节 H3 乙酰化和 H4 脱乙酰化
DOI：
10.1111/nph.18294
复制
发表时间：
2022
期刊：
影响因子：
9.4
通讯作者：
Xu, Jin‐Rong
中科院分区：
文献类型：
--
作者：
Xu, Huaijian;Ye, Meng;Xia, Aliang;Jiang, Hang;Huang, Panpan;Liu, Huiquan;Hou, Rui;Wang, Qinhu;Li, Dongao;Xu, Jin‐Rong
组蛋白乙酰化的稳态水平由组蛋白乙酰转移酶（HAT）和组蛋白脱乙酰酶（HDAC）复合物维持。生长抑制因子（Inhibitor of Growth，ING）蛋白是HAT或HDAC复合物的关键组分，但它们与其他组分的关系以及在植物病原真菌中的作用还没有得到很好的表征。FNG 3的缺失导致真菌发育和致病缺陷。与其他与不同复合物特异性相关的ING蛋白不同，Fng 3与NuA 3 HAT和FgRpd 3 HDAC复合物结合以调节H3乙酰化和H4脱乙酰化，而FgNto 1介导NuA 3复合物中的FgSas 3-Fng 3相互作用，Fng 3与FgRpd 3的C末端区域相互作用，该区域存在于丝状真菌的Rpd 3直系同源物中，但在酵母Rpd 3中不存在。在FgRpd 3的C末端尾部的固有无序区域经历相分离，这对于其与Fng 3的相互作用是重要的。此外，Fng 3的ING结构域决定了其在蛋白质间相互作用和功能上的特异性，通过与两个组蛋白修饰复合物相互作用，参与组蛋白乙酰化的动态调控，对真菌的发育和致病性具有重要意义。
The steady‐state level of histone acetylation is maintained by histone acetyltransferase (HAT) and histone deacetylase (HDAC) complexes. INhibitor of Growth (ING) proteins are key components of the HAT or HDAC complexes but their relationship with other components and roles in phytopathogenic fungi are not well‐characterized.Here, theFNG3ING gene was functionally characterized in the wheat head blight fungusFusarium graminearum. Deletion ofFNG3results in defects in fungal development and pathogenesis. Unlike other ING proteins that are specifically associated with distinct complexes, Fng3 was associated with both NuA3 HAT and FgRpd3 HDAC complexes to regulate H3 acetylation and H4 deacetylation.Whereas FgNto1 mediates the FgSas3–Fng3 interaction in the NuA3 complex, Fng3 interacted with the C‐terminal region of FgRpd3 that is present in Rpd3 orthologs from filamentous fungi but absent in yeast Rpd3. The intrinsically disordered regions in the C‐terminal tail of FgRpd3 underwent phase separation, which was important for its interaction with Fng3. Furthermore, the ING domain of Fng3 is responsible for its specificities in protein–protein interactions and functions.Taken together, Fng3 is involved in the dynamic regulation of histone acetylation by interacting with two histone modification complexes, and is important for fungal development and pathogenicity.