UMMS Affiliation

RNA Therapeutics Institute; Department of Biochemistry and Molecular Pharmacology

Date

4-20-2017

Document Type

Article

Disciplines

Biochemistry | Molecular Biology | Structural Biology

Abstract

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.

Rights and Permissions

Copyright © The Author(s) 2017

DOI of Published Version

10.1038/s41598-017-01186-5

Source

Sci Rep. 2017 Apr 20;7(1):969. doi: 10.1038/s41598-017-01186-5. Link to article on publisher's site

Related Resources

Link to Article in PubMed

Keywords

X-ray crystallography

Journal Title

Scientific reports

PubMed ID

28428565

Creative Commons License

Creative Commons Attribution 4.0 License
This work is licensed under a Creative Commons Attribution 4.0 License.

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