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.
journal_name
Nucleic Acids Resjournal_title
Nucleic acids researchauthors
Guja KE,Venkataraman K,Yakubovskaya E,Shi H,Mejia E,Hambardjieva E,Karzai AW,Garcia-Diaz Mdoi
10.1093/nar/gkt547subject
Has Abstractpub_date
2013-09-01 00:00:00pages
7947-59issue
16eissn
0305-1048issn
1362-4962pii
gkt547journal_volume
41pub_type
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