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.
Document Type
Article
Publication Date
4-29-2025
Digital Object Identifier (DOI)
https://doi.org/10.1038/s41467-025-58692-8
Repository Citation
Rahman, Mohammad M; Zamakhaeva, Svetlana; Rush, Jeffrey S.; Chaton, Catherine T; Kenner, Cameron W; Hla, Yin Mon; Tsui, Ho-Ching Tiffany; Uversky, Vladimir N; Winkler, Malcolm E; Korotkov, Konstantin V; and Korotkova, Natalia, "Glycosylation of serine/threonine-rich intrinsically disordered regions of membrane-associated proteins in streptococci." (2025). Molecular and Cellular Biochemistry Faculty Publications. 199.
https://uknowledge.uky.edu/biochem_facpub/199
Notes/Citation Information
Nat Commun. 2025 Apr 29;16(1):4011