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On August 11, 2021, the authoritative journal of the American Chemical Society " Journal of the American Chemical Society " (JACS) published an online publication titled "Conformational expansion of Tau in condensates promotes" by the Sarah Perrett research group of the Institute of Biophysics of the Chinese Academy of Sciences.
"irversible aggregation" research paper
.
This study uses single-molecule fluorescence technology to reveal the dynamic changes in the conformation of Tau protein during the liquid-liquid phase separation process and the molecular mechanism related to the occurrence of irreversible amyloid aggregation
The phase transition of biological macromolecules has been an emerging research hotspot in the field of biology in recent years.
Through liquid-liquid phase separation, biological macromolecules can be dynamically assembled into membraneless organelles and perform a variety of important biological functions
.
Most proteins involved in phase separation contain low-complexity regions or natural disordered regions, and their abnormal liquid-liquid phase separation and liquid-solid phase transition can lead to disease
Single-molecule fluorescence technology has the advantage of detecting the sub-component distribution and dynamic transformation of macromolecules in the ensemble system, and is a powerful tool for studying the conformation and dynamics of intrinsically disordered proteins (IDP)
.
In recent years, the research team has carried out a series of research work on protein conformational dynamics and interaction mechanisms ( ChemComm 2017; PNAS 2020), and molecular mechanisms of protein amyloid aggregation ( JACS 2018; Nanoscale 2020) using single-molecule fluorescence technology as the main research method .
In this study, we used single-molecule FRET technology and fluorescence correlation spectroscopy (FCS) to study the intramolecular conformational changes and intermolecular interactions during the phase separation of Tau protein
.
The results showed that in the phase-separated state of the Tau protein, its N-terminal and C-terminal domains were opened, exposing the microtubule binding region in the middle
Researcher Ke Sha and associate researcher Wu Si of the Institute of Biophysics of the Chinese Academy of Sciences are the co-corresponding authors of this article.
Doctoral student Wen Jitao in Ke Sha’s group is the first author of this article.
Data analysis and processing have also contributed to this research work
.
The research was funded by the Ministry of Science and Technology and the National Natural Science Foundation of China
Figure Single-molecule FRET and FCS technology to study the conformational changes of Tau protein in the phase-separated state and its relationship with irreversible fibrosis
Article link: https://pubs.
(Contribution: Sarah Perrett Research Group)
