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Recently, the top academic journal "Science" published a latest paper from the protein science research team of the State Key Laboratory of Crop Genetic Improvement of Huazhong Agricultural University and the School of Life Science and Technology
.
The team led by Professor Yin Ping revealed the assembly process of the mitochondrial outer membrane (TOM) translocase complex and clarified the molecular mechanism of the mitochondrial sorting assembly machine (SAM) assisting in the assembly and release of this complex
In humans, the TOM translocase complex is associated with some mitochondrial diseases, such as Parkinson's disease
.
Elucidating the assembly mechanism of the TOM translocase complex will help provide clues for the development of therapeutics for the treatment of mitochondrial diseases
As the energy metabolism "factory" of eukaryotic cells, mitochondria are vital to the normal growth and development of animals and plants
.
The operation of mitochondria requires more than 1,000 proteins, 99% of which are encoded by nuclear genes
The TOM translocase complex consists of 7 subunits, including the core channel Tom40 (beta barrel membrane protein) and 6 transmembrane proteins-regulatory proteins Tom5, Tom6 and Tom7, and receptor proteins Tom20, Tom22 and Tom70
.
In the absence of Tom70 and Tom20, the remaining subunits form a stable TOM core complex
The assembly of the TOM translocase complex is a multi-step and highly dynamic process
.
Previous studies have shown that its assembly requires the assistance of the mitochondrial outer membrane SAM complex, but the specific molecular mechanism of how to assist is not clear
In this research, scientists cleverly designed experiments to "freeze" this high-speed assembly process
.
They found that putting the "parts" of the TOM translocase complex in yeast into the mitochondria of human embryonic kidney cells, the assembly process was stalled as if the pause button was pressed, thus cracking the field that has been unable to capture transients for many years.
The researchers captured multiple intermediate states during the assembly process of the TOM core complex and obtained protein samples
.
Subsequently, single-particle cryo-electron microscopy technology was used to analyze the high-resolution three-dimensional structure of two important intermediate states for the first time
The results showed that Sam37 stabilized the mature Tom40 mainly through electrostatic interaction, thereby promoting the subsequent TOM assembly; Tom7 would promote the assembled Tom40/Tom5/Tom6 to break away from the SAM complex
▲Assembly process of TOM translocase core complex (picture source: reference [3])
Note: The original text has been deleted
Reference materials:
[1] Qiang Wang et al.
[2] Zeyuan Guan et al.
(2021) Structural insights into assembly of human mitochondrial translocase TOM complex.
Cell Discovery.
Doi: 10.
1038/s41421-021-00252-7
[3] "Science" published online research results of the protein science research team of Professor Yin Ping, a member of the China Democratic League of our school.
Retrieved Sep.
6, 2021 from https://tzb.
hzau.
edu.
cn/info/1015/3246.
htm
