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Nanhu News Network (Reporter Wang Qiang) In the early morning of August 27, 2021, Beijing time, Professor Yin Ping's research team from the Hubei Hongshan Laboratory, the State Key Laboratory of Crop Genetic Improvement and the School of Life Science and Technology published a topic online in Science A research paper on "Structural insight into the SAM-mediated assembly of mitochondrial TOM core complex", revealing the molecular mechanism of the assembly of the mitochondrial outer membrane TOM translocase complex
.
Mitochondria are the main sites of eukaryotic energy metabolism and are closely related to the growth and development of plants and animals
.
The life activities of mitochondria require the participation of as many as 1,000 proteins.
In order to explore the assembly mechanism of the TOM translocase complex, the research team used a unique method to reconstruct the assembly process using a mammalian cell recombinant expression system and achieve precise control.
The assembly was artificially assembled by pressing the "pause button
.
" This method allows researchers to capture multiple intermediate states of the TOM assembly process and obtain protein samples, which has overcome many years of problems in the field
It is reported that the research team first reported the composition of the mitochondrial inner membrane TIM22 translocase complex in Cell Research on September 8, 2020, and reported the outer mitochondrial membrane in Cell Discovery on April 13, 2021.
The dimer and trimer transition regulation mechanism of TOM translocase complex
.
The assembly mechanism of the TOM translocase complex reported by Science this time is another breakthrough for the research team to focus on the molecular mechanism of mitochondrial protein transport and sorting
Dr.
Wang Qiang, Dr.
Guan Zeyuan, and Dr.
Qi Liangbo from the School of Biological Sciences of our school are the co-first authors of the paper, Professor Yin Ping is the corresponding author of the paper, and researcher Yan Chuangye from Tsinghua University participated in the research
.
The school-level protein platform provides strong support for the development of this research
Original link:
https://science.
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