The RNA-bound proteome of MRSA reveals post-transcriptional roles for helix-turn-helix DNA-binding and Rossmann-fold proteins

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 compleme...

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Published inNature communications Vol. 13; no. 1; pp. 2883 - 18
Main Authors Chu, Liang-Cui, Arede, Pedro, Li, Wei, Urdaneta, Erika C., Ivanova, Ivayla, McKellar, Stuart W., Wills, Jimi C., Fröhlich, Theresa, von Kriegsheim, Alexander, Beckmann, Benedikt M., Granneman, Sander
Format Journal Article
LanguageEnglish
Published London Nature Publishing Group UK 24.05.2022
Nature Publishing Group
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Summary: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. RNA-binding proteins play key roles in controlling gene expression in many organisms. Here, Chu et al. identify hundreds of RNA-binding proteins in methicillin-resistant Staphylococcus aureus , and show that a major transcription factor uses its helix-turn-helix domain to bind RNAs near intrinsic transcription terminators.
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ISSN:2041-1723
2041-1723
DOI:10.1038/s41467-022-30553-8