TY - JOUR
T1 - Staphylococcus aureus and bacillus subtilis W23 make polyribitol wall teichoic acids using different enzymatic pathways
AU - Brown, Stephanie
AU - Meredith, Timothy
AU - Swoboda, Jonathan
AU - Walker, Suzanne
N1 - Funding Information:
We would like to thank Yuriy Rebets and David Rudner for helpful discussions on gene deletions; Emma Doud for assistance with mass spectrometry analysis; Jennifer Campbell for allowing us to modify her WTA schematic; and Deborah Perlstein for a critical reading of this manuscript. This research was funded by the NIH (1P01AI083214 and 5R01M078477 to S.W., and F3178727 to J.S.).
PY - 2010/10/29
Y1 - 2010/10/29
N2 - Wall teichoic acids (WTAs) are anionic polymers that play key roles in bacterial cell shape, cell division, envelope integrity, biofilm formation, and pathogenesis. B. subtilis W23 and S. aureus both make polyribitol-phosphate (RboP) WTAs and contain similar sets of biosynthetic genes. We use in vitro reconstitution combined with genetics to show that the pathways for WTA biosynthesis in B. subtilis W23 and S. aureus are different. S. aureus requires a glycerol-phosphate primase called TarF in order to make RboP-WTAs; B. subtilis W23 contains a TarF homolog, but this enzyme makes glycerol-phosphate polymers and is not involved in RboP-WTA synthesis. Instead, B. subtilis TarK functions in place of TarF to prime the WTA intermediate for chain extension by TarL. This work highlights the enzymatic diversity of the poorly characterized family of phosphotransferases involved in WTA biosynthesis in Gram-positive organisms.
AB - Wall teichoic acids (WTAs) are anionic polymers that play key roles in bacterial cell shape, cell division, envelope integrity, biofilm formation, and pathogenesis. B. subtilis W23 and S. aureus both make polyribitol-phosphate (RboP) WTAs and contain similar sets of biosynthetic genes. We use in vitro reconstitution combined with genetics to show that the pathways for WTA biosynthesis in B. subtilis W23 and S. aureus are different. S. aureus requires a glycerol-phosphate primase called TarF in order to make RboP-WTAs; B. subtilis W23 contains a TarF homolog, but this enzyme makes glycerol-phosphate polymers and is not involved in RboP-WTA synthesis. Instead, B. subtilis TarK functions in place of TarF to prime the WTA intermediate for chain extension by TarL. This work highlights the enzymatic diversity of the poorly characterized family of phosphotransferases involved in WTA biosynthesis in Gram-positive organisms.
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U2 - 10.1016/j.chembiol.2010.07.017
DO - 10.1016/j.chembiol.2010.07.017
M3 - Article
C2 - 21035733
AN - SCOPUS:78049405519
SN - 1074-5521
VL - 17
SP - 1101
EP - 1110
JO - Chemistry and Biology
JF - Chemistry and Biology
IS - 10
ER -