NMR resonance assignments for the SAM/SAH-binding riboswitch RNA bound to S-adenosylhomocysteine

• Published in: Biomolecular NMR assignments 2018-10, Vol.12 (2), p.329-334
• Main Authors: Weickhmann, A. Katharina, Keller, Heiko, Duchardt-Ferner, Elke, Strebitzer, Elisabeth, Juen, Michael A., Kremser, Johannes, Wurm, Jan Philip, Kreutz, Christoph, Wöhnert, Jens
• Format: Article
• Language: English
• Subjects: Adenosylmethionine; Biochemistry; Biological and Medical Physics; Biophysics; Ligands; Magnetic resonance spectroscopy; Metabolites; NMR; Nuclear magnetic resonance; Nuclear Magnetic Resonance, Biomolecular; Nucleic Acid Conformation; Physics; Physics and Astronomy; Polymer Sciences; Protein structure; Resonance; Ribonucleic acid; Riboswitch; Riboswitches; RNA; S-Adenosylhomocysteine - metabolism; S-Adenosylmethionine; S-Adenosylmethionine - metabolism; Secondary structure; Transcription
• ISSN: 1874-2718; 1874-270X
• DOI: 10.1007/s12104-018-9834-3

Riboswitches are structured RNA elements in the 5′-untranslated regions of bacterial mRNAs that are able to control the transcription or translation of these mRNAs in response to the specific binding of small molecules such as certain metabolites. Riboswitches that bind with high specificity to either S-adenosylmethionine (SAM) or S-adenosylhomocysteine (SAH) are widespread in bacteria. Based on differences in secondary structure and sequence these riboswitches can be grouped into a number of distinct classes. X-ray structures for riboswitch RNAs in complex with SAM or SAH established a structural basis for understanding ligand recognition and discrimination in many of these riboswitch classes. One class of riboswitches—the so-called SAM/SAH riboswitch class—binds SAM and SAH with similar affinity. However, this class of riboswitches is structurally not yet characterized and the structural basis for its unusual bispecificity is not established. In order to understand the ligand recognition mode that enables this riboswitch to bind both SAM and SAH with similar affinities, we are currently determining its structure in complex with SAH using NMR spectroscopy. Here, we present the NMR resonance assignment of the SAM/SAH binding riboswitch (env9b) in complex with SAH as a prerequisite for a solution NMR-based high-resolution structure determination.