化学
混溶性
序列(生物学)
国家(计算机科学)
固态
纳米技术
化学物理
聚合物
有机化学
算法
物理化学
生物化学
材料科学
计算机科学
作者
Ushnish Rana,Ke Xu,Amal Narayanan,Mackenzie T. Walls,Athanassios Z. Panagiotopoulos,José L. Avalos,Clifford P. Brangwynne
标识
DOI:10.1038/s41557-024-01456-6
摘要
Abstract Endogenous biomolecular condensates, composed of a multitude of proteins and RNAs, can organize into multiphasic structures with compositionally distinct phases. This multiphasic organization is generally understood to be critical for facilitating their proper biological function. However, the biophysical principles driving multiphase formation are not completely understood. Here we use in vivo condensate reconstitution experiments and coarse-grained molecular simulations to investigate how oligomerization and sequence interactions modulate multiphase organization in biomolecular condensates. We demonstrate that increasing the oligomerization state of an intrinsically disordered protein results in enhanced immiscibility and multiphase formation. Interestingly, we find that oligomerization tunes the miscibility of intrinsically disordered proteins in an asymmetric manner, with the effect being more pronounced when the intrinsically disordered protein, exhibiting stronger homotypic interactions, is oligomerized. Our findings suggest that oligomerization is a flexible biophysical mechanism that cells can exploit to tune the internal organization of biomolecular condensates and their associated biological functions.
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