Glycosylation of serine/threonine-rich intrinsically disordered regions of membrane-associated proteins in streptococci

Mohammad M. Rahman, Svetlana Zamakhaeva, Jeffrey S. Rush, Catherine T. Chaton, Cameron W. Kenner, Yin Mon Hla, Ho-Ching Tiffany Tsui, Vladimir N. Uversky, Malcolm E. Winkler, Konstantin V. Korotkov and Natalia Korotkova ()
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Mohammad M. Rahman: University of Kentucky
Svetlana Zamakhaeva: University of Kentucky
Jeffrey S. Rush: University of Kentucky
Catherine T. Chaton: University of Kentucky
Cameron W. Kenner: University of Kentucky
Yin Mon Hla: Indiana University Bloomington
Ho-Ching Tiffany Tsui: Indiana University Bloomington
Vladimir N. Uversky: University of South Florida
Malcolm E. Winkler: Indiana University Bloomington
Konstantin V. Korotkov: University of Kentucky
Natalia Korotkova: University of Kentucky

Nature Communications, 2025, vol. 16, issue 1, 1-20

Abstract: Abstract Proteins harboring intrinsically disordered regions (IDRs) lacking stable secondary or tertiary structures are abundant across the three domains of life. These regions have not been systematically studied in prokaryotes. Here, our genome-wide analysis identifies extracytoplasmic serine/threonine-rich IDRs in several biologically important membrane-associated proteins in streptococci. We demonstrate that these IDRs are glycosylated with glucose by glycosyltransferases GtrB and PgtC2 in Streptococcus pyogenes and Streptococcus pneumoniae, and with N-acetylgalactosamine by a Pgf-dependent mechanism in Streptococcus mutans. The absence of glycosylation leads to a defect in biofilm formation under ethanol-stressed conditions in S. mutans. We link this phenotype to the C-terminal IDR of the post-translocation chaperone PrsA. Our data reveal that O-linked glycosylation protects the IDR-containing proteins from proteolytic degradation and is critical for the biological function of PrsA in biofilm formation.

Date: 2025
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DOI: 10.1038/s41467-025-58692-8

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