Small methyltransferase RlmH assembles a composite active site to methylate a ribosomal pseudouridine
UMass Chan Affiliations
Department of Biochemistry and Molecular PharmacologyRNA Therapeutics Institute
Document Type
Journal ArticlePublication Date
2017-04-20
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Eubacterial ribosomal large-subunit methyltransferase H (RlmH) methylates 23S ribosomal RNA pseudouridine 1915 (Psi1915), which lies near the ribosomal decoding center. The smallest member of the SPOUT superfamily of methyltransferases, RlmH lacks the RNA recognition domain found in larger methyltransferases. The catalytic mechanism of RlmH enzyme is unknown. Here, we describe the structures of RlmH bound to S-adenosyl-methionine (SAM) and the methyltransferase inhibitor sinefungin. Our structural and biochemical studies reveal catalytically essential residues in the dimer-mediated asymmetrical active site. One monomer provides the SAM-binding site, whereas the conserved C-terminal tail of the second monomer provides residues essential for catalysis. Our findings elucidate the mechanism by which a small protein dimer assembles a functionally asymmetric architecture.Source
Sci Rep. 2017 Apr 20;7(1):969. doi: 10.1038/s41598-017-01186-5. Link to article on publisher's siteDOI
10.1038/s41598-017-01186-5Permanent Link to this Item
http://hdl.handle.net/20.500.14038/40336PubMed ID
28428565Related Resources
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Copyright © The Author(s) 2017Distribution License
http://creativecommons.org/licenses/by/4.0/ae974a485f413a2113503eed53cd6c53
10.1038/s41598-017-01186-5