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Glycosylation of serine/threonine-rich intrinsically disordered regions of membrane-associated proteins in streptococci
by
Rahman, Mohammad M.
, Uversky, Vladimir N.
, Rush, Jeffrey S.
, Kenner, Cameron W.
, Winkler, Malcolm E.
, Korotkova, Natalia
, Hla, Yin Mon
, Korotkov, Konstantin V.
, Chaton, Catherine T.
, Zamakhaeva, Svetlana
, Tsui, Ho-Ching Tiffany
in
14/19
/ 38/1
/ 38/70
/ 631/326/1320
/ 631/45/221
/ 631/45/470/1981
/ 82/58
/ 82/83
/ Bacteria
/ Bacterial Proteins - chemistry
/ Bacterial Proteins - genetics
/ Bacterial Proteins - metabolism
/ Biofilms
/ Biofilms - growth & development
/ Ethanol
/ Genomic analysis
/ Glucose - metabolism
/ Glycosylation
/ Glycosyltransferases - metabolism
/ Humanities and Social Sciences
/ Intrinsically Disordered Proteins - chemistry
/ Intrinsically Disordered Proteins - genetics
/ Intrinsically Disordered Proteins - metabolism
/ Membrane proteins
/ Membrane Proteins - chemistry
/ Membrane Proteins - genetics
/ Membrane Proteins - metabolism
/ Membranes
/ multidisciplinary
/ N-Acetylgalactosamine
/ Phenotypes
/ Prokaryotes
/ Proteins
/ Proteolysis
/ Science
/ Science (multidisciplinary)
/ Serine
/ Serine - chemistry
/ Serine - metabolism
/ Streptococcus - genetics
/ Streptococcus - metabolism
/ Streptococcus infections
/ Streptococcus mutans
/ Streptococcus mutans - genetics
/ Streptococcus mutans - metabolism
/ Streptococcus pneumoniae - genetics
/ Streptococcus pneumoniae - metabolism
/ Streptococcus pyogenes - genetics
/ Streptococcus pyogenes - metabolism
/ Threonine
/ Threonine - chemistry
/ Threonine - metabolism
/ Translocation
2025
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Glycosylation of serine/threonine-rich intrinsically disordered regions of membrane-associated proteins in streptococci
by
Rahman, Mohammad M.
, Uversky, Vladimir N.
, Rush, Jeffrey S.
, Kenner, Cameron W.
, Winkler, Malcolm E.
, Korotkova, Natalia
, Hla, Yin Mon
, Korotkov, Konstantin V.
, Chaton, Catherine T.
, Zamakhaeva, Svetlana
, Tsui, Ho-Ching Tiffany
in
14/19
/ 38/1
/ 38/70
/ 631/326/1320
/ 631/45/221
/ 631/45/470/1981
/ 82/58
/ 82/83
/ Bacteria
/ Bacterial Proteins - chemistry
/ Bacterial Proteins - genetics
/ Bacterial Proteins - metabolism
/ Biofilms
/ Biofilms - growth & development
/ Ethanol
/ Genomic analysis
/ Glucose - metabolism
/ Glycosylation
/ Glycosyltransferases - metabolism
/ Humanities and Social Sciences
/ Intrinsically Disordered Proteins - chemistry
/ Intrinsically Disordered Proteins - genetics
/ Intrinsically Disordered Proteins - metabolism
/ Membrane proteins
/ Membrane Proteins - chemistry
/ Membrane Proteins - genetics
/ Membrane Proteins - metabolism
/ Membranes
/ multidisciplinary
/ N-Acetylgalactosamine
/ Phenotypes
/ Prokaryotes
/ Proteins
/ Proteolysis
/ Science
/ Science (multidisciplinary)
/ Serine
/ Serine - chemistry
/ Serine - metabolism
/ Streptococcus - genetics
/ Streptococcus - metabolism
/ Streptococcus infections
/ Streptococcus mutans
/ Streptococcus mutans - genetics
/ Streptococcus mutans - metabolism
/ Streptococcus pneumoniae - genetics
/ Streptococcus pneumoniae - metabolism
/ Streptococcus pyogenes - genetics
/ Streptococcus pyogenes - metabolism
/ Threonine
/ Threonine - chemistry
/ Threonine - metabolism
/ Translocation
2025
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Glycosylation of serine/threonine-rich intrinsically disordered regions of membrane-associated proteins in streptococci
by
Rahman, Mohammad M.
, Uversky, Vladimir N.
, Rush, Jeffrey S.
, Kenner, Cameron W.
, Winkler, Malcolm E.
, Korotkova, Natalia
, Hla, Yin Mon
, Korotkov, Konstantin V.
, Chaton, Catherine T.
, Zamakhaeva, Svetlana
, Tsui, Ho-Ching Tiffany
in
14/19
/ 38/1
/ 38/70
/ 631/326/1320
/ 631/45/221
/ 631/45/470/1981
/ 82/58
/ 82/83
/ Bacteria
/ Bacterial Proteins - chemistry
/ Bacterial Proteins - genetics
/ Bacterial Proteins - metabolism
/ Biofilms
/ Biofilms - growth & development
/ Ethanol
/ Genomic analysis
/ Glucose - metabolism
/ Glycosylation
/ Glycosyltransferases - metabolism
/ Humanities and Social Sciences
/ Intrinsically Disordered Proteins - chemistry
/ Intrinsically Disordered Proteins - genetics
/ Intrinsically Disordered Proteins - metabolism
/ Membrane proteins
/ Membrane Proteins - chemistry
/ Membrane Proteins - genetics
/ Membrane Proteins - metabolism
/ Membranes
/ multidisciplinary
/ N-Acetylgalactosamine
/ Phenotypes
/ Prokaryotes
/ Proteins
/ Proteolysis
/ Science
/ Science (multidisciplinary)
/ Serine
/ Serine - chemistry
/ Serine - metabolism
/ Streptococcus - genetics
/ Streptococcus - metabolism
/ Streptococcus infections
/ Streptococcus mutans
/ Streptococcus mutans - genetics
/ Streptococcus mutans - metabolism
/ Streptococcus pneumoniae - genetics
/ Streptococcus pneumoniae - metabolism
/ Streptococcus pyogenes - genetics
/ Streptococcus pyogenes - metabolism
/ Threonine
/ Threonine - chemistry
/ Threonine - metabolism
/ Translocation
2025
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Glycosylation of serine/threonine-rich intrinsically disordered regions of membrane-associated proteins in streptococci
Journal Article
Glycosylation of serine/threonine-rich intrinsically disordered regions of membrane-associated proteins in streptococci
2025
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Overview
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.
Here, the authors identify mechanisms of glycosylation of intrinsically disordered regions present in streptococci membrane proteins, uncovering a functional role for glycosylation in
Streptococcus mutans
chaperone PrsA.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 38/1
/ 38/70
/ 82/58
/ 82/83
/ Bacteria
/ Bacterial Proteins - chemistry
/ Bacterial Proteins - genetics
/ Bacterial Proteins - metabolism
/ Biofilms
/ Biofilms - growth & development
/ Ethanol
/ Glycosyltransferases - metabolism
/ Humanities and Social Sciences
/ Intrinsically Disordered Proteins - chemistry
/ Intrinsically Disordered Proteins - genetics
/ Intrinsically Disordered Proteins - metabolism
/ Membrane Proteins - chemistry
/ Membrane Proteins - genetics
/ Membrane Proteins - metabolism
/ Proteins
/ Science
/ Serine
/ Streptococcus mutans - genetics
/ Streptococcus mutans - metabolism
/ Streptococcus pneumoniae - genetics
/ Streptococcus pneumoniae - metabolism
/ Streptococcus pyogenes - genetics
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