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| Scientists discover new factors in response to stress in rice endoplasmic reticulum |
Recently, Qu Leqing’s team, a researcher at the Institute of Botany, Chinese Academy of Sciences, discovered that OsFes1C is a nucleotide exchange factor of OsBiP1.
Rice plants that overexpress or inhibit the expression of OsFes1C are more sensitive to endoplasmic reticulum stress and their growth and development are inhibited
.
This study revealed the molecular mechanism of OsFes1C regulating OsBiP1, and deepened the understanding of rice endoplasmic reticulum stress response mechanisms
Immunoglobulin binding protein (BiP) is the main molecular chaperone in the cavity of the endoplasmic reticulum.
It is involved in protein folding, modification, transmembrane transport, and degradation of misfolded proteins.
It is involved in the protein quality control and stress response mediated by the endoplasmic reticulum.
Play an important role
.
The function of BiP requires the co-action of auxiliary chaperone protein and nucleotide exchange factor (NEF), which directly regulates the binding and release of BiP and protein
When the researchers analyzed the endoplasmic reticulum-stressed rice seeds by proteomics, they identified a protein OsFes1C whose expression level was extremely significantly up-regulated
.
This protein is homologous to Fes1p in yeast and mammals, but is different from Fes1p in cytoplasm and response to heat stress.
They further researched and found that OsFes1C can directly interact with OsBiP1
.
Adding ADP can enhance the interaction between OsFes1C and OsBiP1, while adding ATP weakens the interaction
This research was supported by the Chinese Academy of Sciences Strategic Leading Science and Technology Special Class A, the National Major Special Project for Cultivating New Varieties of Genetically Modified Organisms, and the National Natural Science Foundation of China
.
(Source: Tian Ruiying, China Science News)
Related paper information: https://doi.
https://doi.
org/10.
1093/plphys/kiab263 https://doi.
org/10.
1093/plphys/kiab263
