ArticleNucleic acids research2015
Structure of mitochondrial poly(A) RNA polymerase reveals the structural basis for dimerization, ATP selectivity and the SPAX4 disease phenotype.
Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Mitochondrial translational control in cardiovascular diseases: from mechanisms to therapies.Redox biology · 2026Review
- Integrative Transcriptomic Analysis Identifies Novel Mitochondrial Gene Targets in Parkinson's Disease.Molecular neurobiology · 2026Article
- Failure to Guard: Mitochondrial Protein Quality Control in Cancer.International journal of molecular sciences · 2021Review
- Functions and mechanisms of RNA tailing by metazoan terminal nucleotidyltransferases.Wiley interdisciplinary reviews. RNA · 2021Review
- Identification of Parkinson's Disease-Causing Genes via Omics Data.Frontiers in genetics · 2021Article
- Single-Cell Approaches for Studying the Role of Mitochondrial DNA in Neurodegenerative Disease.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Review
- Structures of mammalian GLD-2 proteins reveal molecular basis of their functional diversity in mRNA and microRNA processing.Nucleic acids research · 2020Article
- FAM46B is a prokaryotic-like cytoplasmic poly(A) polymerase essential in human embryonic stem cells.Nucleic acids research · 2020Article
- Crystal structure of the Lin28-interacting module of human terminal uridylyltransferase that regulates let-7 expression.Nature communications · 2019Article
- Article
- Mitochondrial transcription and translation: overview.Essays in biochemistry · 2018Review
- Function and Regulation of Human Terminal Uridylyltransferases.Frontiers in genetics · 2018Review
- Biochemical and structural bioinformatics studies of fungal CutA nucleotidyltransferases explain their unusual specificity toward CTP and increased tendency for cytidine incorporation at the 3'-terminal positions of synthesized tails.RNA (New York, N.Y.) · 2017Article
- Multi-domain utilization by TUT4 and TUT7 in control of let-7 biogenesis.Nature structural & molecular biology · 2017Article
- Crystal structures of U6 snRNA-specific terminal uridylyltransferase.Nature communications · 2017Article
- SnoN Stabilizes the SMAD3/SMAD4 Protein Complex.Scientific reports · 2017Article
- RNA Editing TUTase 1: structural foundation of substrate recognition, complex interactions and drug targeting.Nucleic acids research · 2016Article
- Mitochondrial Polyadenylation Is a One-Step Process Required for mRNA Integrity and tRNA Maturation.PLoS genetics · 2016Article
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2 authors.
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Abstract
Polyadenylation, performed by poly(A) polymerases (PAPs), is a ubiquitous post-transcriptional modification that plays key roles in multiple aspects of RNA metabolism. Although cytoplasmic and nuclear PAPs have been studied extensively, the mechanism by which mitochondrial PAP (mtPAP) selects adenosine triphosphate over other nucleotides is unknown. Furthermore, mtPAP is unique because it acts as a dimer. However, mtPAP's dimerization requirement remains enigmatic. Here, we show the structural basis for mtPAP's nucleotide selectivity, dimerization and catalysis. Our structures reveal an intricate dimerization interface that features an RNA-recognition module formed through strand complementation. Further, we propose the structural basis for the N478D mutation that drastically reduces the length of poly(A) tails on mitochondrial mRNAs in patients with spastic ataxia 4 (SPAX4), a severe and progressive neurodegenerative disease.
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