Distinct pathogenic mechanisms of various RARS1 mutations in Pelizaeus-Merzbacher-like disease.

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Tytuł:: Distinct pathogenic mechanisms of various RARS1 mutations in Pelizaeus-Merzbacher-like disease.
Autorzy:: Li G; State Key Laboratory of Molecular Biology, CAS Center for Excellence in Molecular Cell Science, Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, University of Chinese Academy of Sciences, Shanghai, 200031, China.
Eriani G; Architecture et Réactivité de l'ARN, UPR9002 CNRS, Institut de Biologie Moléculaire et Cellulaire, Université de Strasbourg, 67084, Strasbourg, France.
Wang ED; State Key Laboratory of Molecular Biology, CAS Center for Excellence in Molecular Cell Science, Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, University of Chinese Academy of Sciences, Shanghai, 200031, China. .; School of Life Science and Technology, ShanghaiTech University, Shanghai, 201210, China. .
Zhou XL; State Key Laboratory of Molecular Biology, CAS Center for Excellence in Molecular Cell Science, Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, University of Chinese Academy of Sciences, Shanghai, 200031, China. .
Źródło:: Science China. Life sciences [Sci China Life Sci] 2021 Oct; Vol. 64 (10), pp. 1645-1660. Date of Electronic Publication: 2021 Jan 28.
Typ publikacji:: Journal Article
Język:: English
Imprint Name(s):: Original Publication: Beijing : Science China Press, co-published with Springer
MeSH Terms:: Arginine-tRNA Ligase/*genetics
Hereditary Central Nervous System Demyelinating Diseases/*genetics
5' Untranslated Regions ; Arginine-tRNA Ligase/chemistry ; Arginine-tRNA Ligase/metabolism ; Humans ; Mutation ; Open Reading Frames ; Protein Biosynthesis ; Protein Conformation ; Protein Domains ; Protein Stability
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Contributed Indexing:: Keywords: aminoacyl-tRNA synthetase (aaRS); central nervous system (CNS); protein biosynthesis; tRNA; translation initiation
Substance Nomenclature:: 0 (5' Untranslated Regions)
EC 6.1.1.19 (Arginine-tRNA Ligase)
SCR Disease Name:: Leukodystrophy, Hypomyelinating, 2
Entry Date(s):: Date Created: 20210130 Date Completed: 20220308 Latest Revision: 20220308
Update Code:: 20240104
DOI:: 10.1007/s11427-020-1838-2
PMID:: 33515434
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Mutations of the genes encoding aminoacyl-tRNA synthetases are highly associated with various central nervous system disorders. Recurrent mutations, including c.5A>G, p.D2G; c.1367C>T, p.S456L; c.1535G>A, p.R512Q and c.1846_1847del, p. Y616Lfs*6 of RARS1 gene, which encodes two forms of human cytoplasmic arginyl-tRNA synthetase (hArgRS), are linked to Pelizaeus-Merzbacher-like disease (PMLD) with unclear pathogenesis. Among these mutations, c.5A>G is the most extensively reported mutation, leading to a p.D2G mutation in the N-terminal extension of the long-form hArgRS. Here, we showed the detrimental effects of R512Q substitution and ΔC mutations on the structure and function of hArgRS, while the most frequent mutation c.5A>G, p.D2G acted in a different manner without impairing hArgRS activity. The nucleotide substitution c.5A>G reduced translation of hArgRS mRNA, and an upstream open reading frame contributed to the suppressed translation of the downstream main ORF. Taken together, our results elucidated distinct pathogenic mechanisms of various RARS1 mutations in PMLD.
(© 2021. Science China Press and Springer-Verlag GmbH Germany, part of Springer Nature.)

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