{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Chu LC"],"funding":["Deutsche Forschungsgemeinschaft","Medical Research Council","Boehringer Ingelheim Stiftung","Wellcome Trust"],"pagination":["2883"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9130240"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["13(1)"],"pubmed_abstract":["RNA-binding proteins play key roles in controlling gene expression in many organisms, but relatively few have been identified and characterised in detail in Gram-positive bacteria. Here, we globally analyse RNA-binding proteins in methicillin-resistant Staphylococcus aureus (MRSA) using two complementary biochemical approaches. We identify hundreds of putative RNA-binding proteins, many containing unconventional RNA-binding domains such as Rossmann-fold domains. Remarkably, more than half of the proteins containing helix-turn-helix (HTH) domains, which are frequently found in prokaryotic transcription factors, bind RNA in vivo. In particular, the CcpA transcription factor, a master regulator of carbon metabolism, uses its HTH domain to bind hundreds of RNAs near intrinsic transcription terminators in vivo. We propose that CcpA, besides acting as a transcription factor, post-transcriptionally regulates the stability of many RNAs."],"journal":["Nature communications"],"pubmed_title":["The RNA-bound proteome of MRSA reveals post-transcriptional roles for helix-turn-helix DNA-binding and Rossmann-fold proteins."],"pmcid":["PMC9130240"],"funding_grant_id":["208402/Z/17/Z","MR/R008205/1","109093/Z/15/A","IRTG 2290"],"pubmed_authors":["Li W","Frohlich T","von Kriegsheim A","Chu LC","Urdaneta EC","McKellar SW","Ivanova I","Granneman S","Arede P","Wills JC","Beckmann BM"],"additional_accession":[]},"is_claimable":false,"name":"The RNA-bound proteome of MRSA reveals post-transcriptional roles for helix-turn-helix DNA-binding and Rossmann-fold proteins.","description":"RNA-binding proteins play key roles in controlling gene expression in many organisms, but relatively few have been identified and characterised in detail in Gram-positive bacteria. Here, we globally analyse RNA-binding proteins in methicillin-resistant Staphylococcus aureus (MRSA) using two complementary biochemical approaches. We identify hundreds of putative RNA-binding proteins, many containing unconventional RNA-binding domains such as Rossmann-fold domains. Remarkably, more than half of the proteins containing helix-turn-helix (HTH) domains, which are frequently found in prokaryotic transcription factors, bind RNA in vivo. In particular, the CcpA transcription factor, a master regulator of carbon metabolism, uses its HTH domain to bind hundreds of RNAs near intrinsic transcription terminators in vivo. We propose that CcpA, besides acting as a transcription factor, post-transcriptionally regulates the stability of many RNAs.","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 May","modification":"2026-05-09T23:39:33.272Z","creation":"2025-04-04T19:33:20.246Z"},"accession":"S-EPMC9130240","cross_references":{"pubmed":["35610211"],"doi":["10.1038/s41467-022-30553-8"]}}