Small methyltransferase RlmH assembles a composite active site to methylate a ribosomal pseudouridine
UMass Chan AffiliationsDepartment of Biochemistry and Molecular Pharmacology
RNA Therapeutics Institute
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AbstractEubacterial 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.
SourceSci Rep. 2017 Apr 20;7(1):969. doi: 10.1038/s41598-017-01186-5. Link to article on publisher's site
Permanent Link to this Itemhttp://hdl.handle.net/20.500.14038/40336
RightsCopyright © The Author(s) 2017