Advances in the study of pathogenic molecular mechanisms of mutonic ational mutations of mitochondrial tRNA pathogenic points.

On April 10, the international academic journal Nucleic Acid Research published its latest research from wang Endo Research Group, Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences: A non-non-Watson-Crick base in hmtRNAThrs r and functional eithiosis to local.
mitochondria are the key organininin in eukaryotic cells, regulating normal life activity.
mitochondria have their own genomes and complete translation machines.
mitochondrial gene mutations are associated with a variety of mitochondrial diseases.
human mitochondria susteintRNA (hmtRNAThr) is encoded by the mitochondrial genome, with only one gene copy, and is responsible for decoding all Suthine crypts in the mitochondrial translation system, which is of great significance to mitochondria structure, function and steady state.
currently, there are six pathogenic site mutations found in the hmtRNAThr gene, which are likely to affect the structure and function of tRNA, and thus the biosynthesis of mitochondrial proteins, but the specific pathogenic molecular mechanism is completely unknown.
Under the co-guidance of researchers Wang Endo and Zhou Xiaolong, Ph.D. candidate Wang Yong and others focused on the two pathogenic sites of The Mutations G30A and A38G, which are located in tRNA anti-cryptocode stems and rings that have a significant impact on the tRNA structure and aminoization function.
in evolution, the third pair of the hmtRNAThr anti-coded stem has evolved a non-Watson-Crick base pair of A29/C41 different from primates such as chimpanzees, highlighting the critical importance of the fourth pair of Watson-Crick base pairs of The R30-C40 to maintain tRNA structure and function.
disease-causing site mutation G30A destroys the anti-crypto-stalks fourth pair of Watson-Crick base pair G30-C40, affecting the structure, function and post-transcription modification of tRNA.
a disease-causing mutation A38G at a disease point located in an anti-password ring and close to an anti-password son impairs the ability of tRNA to receive amino acids and a missing A37-bit transcription to ensure translation accuracy.
indicates that the mutations G30A and A38G at the site of the disease caused the reduction of raw materials for protein synthesis and the decrease in the accuracy of translation.
the study explains the increased efficiency and fidelity of the disease-causing site mutationSG30A and A38G, which lead to the occurrence of mitochondrial disease, which is of great significance for the in-depth understanding of the pathogenic molecular mechanism of the mitochondrial tRNA pathogenic point mutation.
the research has been funded by the National Key Research and Development Program, the National Natural Science Foundation, the Chinese Academy of Sciences, the Shanghai Science and Technology Commission, etc.
data collection is supported by the Public Technical Service Center for Biochemistry and Cell.
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