# Exploring the Role of the Processing Body in Plant Abiotic Stress Response
## 3 Assembly of P-Body  
### Liquid-Liquid Phase Separation (LLPS) Drives P-Body Assembly  
Most of the proteins in membrane-less organelles (MLOs) are intrinsically disordered proteins or contain intrinsically disordered regions (IDRs) [29]. Some of these IDRs contain binding sites that promote multivalent interactions or a large number of low hydrophobic sequences that have the ability to drive proteins to undergo liquid-liquid phase separation and thus aggregate into MLOs [30,31]. As a type of MLO, the formation of the P-Body is also related to disordered protein structure. Currently, numerous studies focus on the protein components of the P-Body, utilizing bioinformatics predictions and nuclear magnetic resonance (NMR) experiments to analyze its protein structure. Table 1 lists the proteins of the P-Body that have been shown to have disordered regions. The intrinsically disordered structure of these proteins contributes to the proper localization of the proteins and participates in the assembly of the P-Body. PONDR [[http://pondr.com/](http://pondr.com/)]([http://pondr.com/](http://pondr.com/)) (accessed on 28 August 2024) predicts that the serine-rich C-terminal region of the Nst1 protein is disordered in yeast. Compared to the Nst1 protein, the N_st1_ mutants that lack the serine-rich region have inhibited the ability to form P-Bodies [32]. Similarly, in _Arabidopsis_, the SUPPRESSOR WITH MORPHOGENETIC EFFECTS ON GENITALIA 7 (SMG7) protein, which lacks a disordered C-terminus, was unable to correctly localize THREE-DIVISION MUTANT 1 (TDM1) to the P-Body upon interaction with TDM1 [33]. All of these results indicate that the intrinsically disordered structure of the proteins is essential for the formation of the P-Body. In addition to intrinsically disordered regions (IDRs), proteins in the P-Body typically contain low-complexity sequences, RNA-binding activity, and pr \begin{table}
\begin{tabular}{c c c c c} \hline \hline
**Protein** & **Uniprot** & **Experimental Method** & **Species** & **References** \\ \hline DCP1 & AC294554.1 & Prediction & _D. melanogaster_ & [34] \\ DCP2 & AFH04447.1 & Prediction & _D. melanogaster_ & [34,35] \\ DCP5 & OAP16255.1 & predicted by D2P2 & _A. thaliana_ & [36] \\ Me31B & EDW88764.1 & Prediction & _Drosophila_ & [37] \\ NBDY & NP\_001335058.1 & 1H-15N HSQC & _H. sapiens_ & [38] \\ Sts5 & BAA23619.1 & Prediction & _S. pombe_ & [39] \\ Puf2 & NP\_595389.2 & Prediction & _S. pombe_ & [40] \\ Puf3 & NP\_593141.2 & Prediction & _S. pombe_ & [40] \\ Puf4 & CAB03616.1 & Prediction & _S. pombe_ & [40] \\ SMG7 & OAO95115.1 & Prediction & _A. thaliana_ & [33] \\ Lsm4 & QHB08189.1 & Prediction & _S. cerevisiae_ & [41] \\ Dhh1 & CAA98734.1 & Prediction & _S. cerevisiae_ & [41] \\ Pop2 & CAA96333.1 & Prediction & _S. cerevisiae_ & [41] \\ Ccr4 & AAB24455.1 & Prediction & _S. cerevisiae_ & [41] \\ Nst1 & QHB11286.1 & Prediction & _S. cerevisiae_ & [32] \\ G3 BP & CAG38772.1 & Prediction & _H. sapiens_ & [42] \\ MEG-1 & NP\_510319.1 & Prediction & _C. elegans_ & [43] \\ MEG-2 & NP\_510318.2 & Prediction & _C. elegans_ & [43] \\ \hline \hline \end{tabular}
\end{table} 
Table 1: Proteins containing disordered regions in P-Body. promote LLPS and are crucial in the assembly and maintenance of the P-Body [19]. The RNA-binding proteins aggregate with mRNA to initially form mRNP. To form a larger quantity and size of P-Body, these mRNPs further interacted through domains such as Lsm4 Q/N domain, Edc3 Yief-N domain, or Pat1 N Terminal Domain [19,44]. This complex interaction eventually forms visible particles in the cytoplasm. Yeast strains lacking either _Edc3_ or the (C)-terminal Q/N-rich domain of the _Lsm4_ can still form P-Bodies through another protein driving assembly, but the P-Body in the _Edc3A Lsm4 AC_ double deletion strain is drastically reduced [44]. In addition, [PERSON] et al.