{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Lu C"],"funding":["NCRR NIH HHS","NIGMS NIH HHS"],"pagination":["786-99"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3479645"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["409(5)"],"pubmed_abstract":["The S(MK) box (SAM-III) translational riboswitches were identified in S-adenosyl-l-methionine (SAM) synthetase metK genes in members of Lactobacillales. This riboswitch switches between two alternative conformations in response to intracellular SAM concentration and controls metK expression at the level of translation initiation. We previously reported the crystal structure of the SAM-bound S(MK) box riboswitch. In this study, we combined selective 2'-hydroxyl acylation analyzed by primer extension chemical probing with mutagenesis to probe the ligand-induced conformational switching mechanism. We revealed that while the majority of the apo S(MK) box RNA molecules exist in an alternatively base-paired (ON) conformation, a subset of them pre-organize into a SAM-bound-like (READY) conformati"],"journal":["Journal of molecular biology"],"pubmed_title":["Variable sequences outside the SAM-binding core critically influence the conformational dynamics of the SAM-III/SMK box riboswitch."],"pmcid":["PMC3479645"],"funding_grant_id":["R01 GM063615","R01 GM086766","P41 RR015301","GM086766","GM63615","P41 RR001646"],"pubmed_authors":["Ding F","Smith AM","Lu C","Ke A","Chowdhury A","Henkin TM"],"additional_accession":[]},"is_claimable":false,"name":"Variable sequences outside the SAM-binding core critically influence the conformational dynamics of the SAM-III/SMK box riboswitch.","description":"The S(MK) box (SAM-III) translational riboswitches were identified in S-adenosyl-l-methionine (SAM) synthetase metK genes in members of Lactobacillales. This riboswitch switches between two alternative conformations in response to intracellular SAM concentration and controls metK expression at the level of translation initiation. We previously reported the crystal structure of the SAM-bound S(MK) box riboswitch. In this study, we combined selective 2'-hydroxyl acylation analyzed by primer extension chemical probing with mutagenesis to probe the ligand-induced conformational switching mechanism. We revealed that while the majority of the apo S(MK) box RNA molecules exist in an alternatively base-paired (ON) conformation, a subset of them pre-organize into a SAM-bound-like (READY) conformati","dates":{"release":"2011-01-01T00:00:00Z","publication":"2011 Jun","modification":"2025-04-05T12:54:37.809Z","creation":"2019-03-27T00:59:29Z"},"accession":"S-EPMC3479645","cross_references":{"pubmed":["21549712"],"doi":["10.1016/j.jmb.2011.04.039"]}}