ArticleNucleic acids research2013
Structural basis for S-adenosylmethionine binding and methyltransferase activity by mitochondrial transcription factor B1.
Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 24 citations in OpenAlex.
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- Ribosomal biogenesis regulator DIMT1 controls β-cell protein synthesis, mitochondrial function, and insulin secretion.The Journal of biological chemistry · 2022Article
- A comprehensive review of m6A/m6Am RNA methyltransferase structures.Nucleic acids research · 2021Review
- Mechanisms of mammalian mitochondrial transcription.Protein science : a publication of the Protein Society · 2019Review
- Structural insights into dimethylation of 12S rRNA by TFB1M: indispensable role in translation of mitochondrial genes and mitochondrial function.Nucleic acids research · 2019Article
- Structural basis of mitochondrial transcription.Nature structural & molecular biology · 2018Review
- Article
- Structural Basis for Cooperative Function of Mettl3 and Mettl14 Methyltransferases.Molecular cell · 2016Article
- A model for transcription initiation in human mitochondria.Nucleic acids research · 2015Article
- Mitochondrial m.1584A 12S m62A rRNA methylation in families with m.1555A>G associated hearing loss.Human molecular genetics · 2015Article
- Mitochondrial protein synthesis: figuring the fundamentals, complexities and complications, of mammalian mitochondrial translation.FEBS letters · 2014Review
- Organization of the human mitochondrial transcription initiation complex.Nucleic acids research · 2014Article
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Authors and funding
8 authors at 2 institutions in 1 country.
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Abstract
Eukaryotic transcription factor B (TFB) proteins are homologous to KsgA/Dim1 ribosomal RNA (rRNA) methyltransferases. The mammalian TFB1, mitochondrial (TFB1M) factor is an essential protein necessary for mitochondrial gene expression. TFB1M mediates an rRNA modification in the small ribosomal subunit and thus plays a role analogous to KsgA/Dim1 proteins. This modification has been linked to mitochondrial dysfunctions leading to maternally inherited deafness, aminoglycoside sensitivity and diabetes. Here, we present the first structural characterization of the mammalian TFB1 factor. We have solved two X-ray crystallographic structures of TFB1M with (2.1 Å) and without (2.0 Å) its cofactor S-adenosyl-L-methionine. These structures reveal that TFB1M shares a conserved methyltransferase core with other KsgA/Dim1 methyltransferases and shed light on the structural basis of S-adenosyl-L-methionine binding and methyltransferase activity. Together with mutagenesis studies, these data suggest a model for substrate binding and provide insight into the mechanism of methyl transfer, clarifying the role of this factor in an essential process for mitochondrial function.
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