RRM1 variants cause a mitochondrial DNA maintenance disorder via impaired de novo nucleotide synthesis.
Genetic diseases
Genetics
Mitochondria
Molecular pathology
Journal
The Journal of clinical investigation
ISSN: 1558-8238
Titre abrégé: J Clin Invest
Pays: United States
ID NLM: 7802877
Informations de publication
Date de publication:
01 07 2022
01 07 2022
Historique:
received:
04
11
2020
accepted:
19
05
2022
pubmed:
27
5
2022
medline:
6
7
2022
entrez:
26
5
2022
Statut:
ppublish
Résumé
Mitochondrial DNA (mtDNA) depletion/deletions syndromes (MDDS) encompass a clinically and etiologically heterogenous group of mitochondrial disorders caused by impaired mtDNA maintenance. Among the most frequent causes of MDDS are defects in nucleoside/nucleotide metabolism, which is critical for synthesis and homeostasis of the deoxynucleoside triphosphate (dNTP) substrates of mtDNA replication. A central enzyme for generating dNTPs is ribonucleotide reductase, a critical mediator of de novo nucleotide synthesis composed of catalytic RRM1 subunits in complex with RRM2 or p53R2. Here, we report 5 probands from 4 families who presented with ptosis and ophthalmoplegia as well as other clinical manifestations and multiple mtDNA deletions in muscle. We identified 3 RRM1 loss-of-function variants, including a dominant catalytic site variant (NP_001024.1: p.N427K) and 2 homozygous recessive variants at p.R381, which has evolutionarily conserved interactions with the specificity site. Atomistic molecular dynamics simulations indicate mechanisms by which RRM1 variants affect protein structure. Cultured primary skin fibroblasts of probands manifested mtDNA depletion under cycling conditions, indicating impaired de novo nucleotide synthesis. Fibroblasts also exhibited aberrant nucleoside diphosphate and dNTP pools and mtDNA ribonucleotide incorporation. Our data reveal that primary RRM1 deficiency and, by extension, impaired de novo nucleotide synthesis are causes of MDDS.
Identifiants
pubmed: 35617047
pii: 145660
doi: 10.1172/JCI145660
pmc: PMC9246377
doi:
pii:
Substances chimiques
DNA, Mitochondrial
0
Nucleosides
0
Nucleotides
0
Ribonucleotide Reductases
EC 1.17.4.-
RRM1 protein, human
EC 1.17.4.1
Ribonucleoside Diphosphate Reductase
EC 1.17.4.1
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Medical Research Council
ID : MR/S005021/1
Pays : United Kingdom
Organisme : NINDS NIH HHS
ID : U54 NS078059
Pays : United States
Organisme : Wellcome Trust
ID : 203105/Z/16/Z
Pays : United Kingdom
Organisme : NIGMS NIH HHS
ID : R35 GM139453
Pays : United States
Organisme : Wellcome Trust
Pays : United Kingdom
Organisme : NINDS NIH HHS
ID : R01 NS083726
Pays : United States
Organisme : NICHD NIH HHS
ID : P01 HD032062
Pays : United States
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