The S65 of the ubigen monos unit is regulated by pH after phosphorylation.

On June 13th, a research team led by Tang Wei, a researcher at the Wuhan Institute of Physics and Mathematics of the Chinese Academy of Sciences, published a research paper entitled Ubiquitin S65 Society engenders a pH-sensitive conformation switch online in the Proceedings of the National Academy of Sciences (PNAS).
their work reveals that after the S65 of the ubigen monos are phosphorylated, four kinds of images can be transformed into each other, the three-dimensional structure of each of the structures is analyzed, and the composition of these structures is adjusted by pH.
further, using single-molecule fluorescence techniques, they found that changes in the composition of ubifain monosomes also affected the four-stage structure of the ubifactory chain, resulting in Ubigens being able to bind to different target proteins and perform different functions.
2014 study reported for the first time that ubigen can be phosphated by PINK1 at its S65-bit point, and that phosphorylated ubitin activates PARKIN, causing mitochondrial autophagy, but other biological functions of phosphate ubitin remain unclear.
In the latest PNAS paper, the biomicrobial dynamics research team of Wuhan Institute of Biomagnetic Dynamics used bioMA resonance technology and other biophysical methods to accurately analyze the simultaneous stretch and contraction structure of phosphate ubiquitin, and found that the phosphate groups of phosphate in the stretch state and the shrinked phosphorylated ubiquitin had distinct pKa values, 7.2 and 5.8, respectively.
therefore, when the solution pH is elevated, phosphate ubigen tends to shrink the structure, and when the solution pH decreases, the phosphorylation ubigen tends to stretch the structure.
in cells, different subcellular sites have different pH values, cells in different physiological and pathological states, the local pH also changes.
phosphorylation and ubigenization are two of the most common protein post-translation modifications, phosphorylation can give the structure and function of ubitin sensitivity to the environment pH, this discovery will have a profound impact on biological research.
team of bio-molecular dynamics led by Tang Qi has been engaged in the study of the dynamic structure of ubigen for many years and has completed a series of important discoveries.
We used spectral analysis to find for the first time that there is a very weak non-co-pyrogen interaction between ubiquitin monos units (Angew.Chem., 2012), a non-co-price interaction that regulates the four-stage structure between the ubiquitin chain sub-basees and enables the ubiquitin chain to interact with different structures and functions through the image selection mechanism (eLife, 2015).
polymorphic balance of phosphate ubiquitin in the solution.
As the pH rises (represented by an orange background to a cyan background) phosphorylated ubiquity is de-protonized, it tends to shrink the structure, and as the pH decreases (represented by a cyan background to an orange background) phosphorylation ubiquity is protonized, it tends to stretch the structure.
Xu and Yu Chau, associate researchers of the Bio-Molecular Dynamics Research Team, co-authored the paper.
, who graduated from Wuhan Institute of Bio-Molecular Dynamics Research Group, is currently working at Zhejiang University School of Medicine and participating in the publication of relevant research results as a co-author of the paper.
the study was funded by the Ministry of Science and Technology, the National Natural Science Foundation and the Howard Hughes Medical Research Institute (HHMI) in the United States.
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