Bacterial cell wall biogenesis is mediated by SEDS and PBP polymerase families functioning semi-autonomously

DSpace/Manakin Repository

Bacterial cell wall biogenesis is mediated by SEDS and PBP polymerase families functioning semi-autonomously

Citable link to this page

 

 
Title: Bacterial cell wall biogenesis is mediated by SEDS and PBP polymerase families functioning semi-autonomously
Author: Cho, Hongbaek; Wivagg, Carl N.; Kapoor, Mrinal; Barry, Zachary; Rohs, Patricia D.A.; Suh, Hyunsuk; Marto, Jarrod A.; Garner, Ethan C.; Bernhardt, Thomas G.

Note: Order does not necessarily reflect citation order of authors.

Citation: Cho, Hongbaek, Carl N. Wivagg, Mrinal Kapoor, Zachary Barry, Patricia D.A. Rohs, Hyunsuk Suh, Jarrod A. Marto, Ethan C. Garner, and Thomas G. Bernhardt. 2016. “Bacterial cell wall biogenesis is mediated by SEDS and PBP polymerase families functioning semi-autonomously.” Nature microbiology 1 (1): 16172. doi:10.1038/nmicrobiol.2016.172. http://dx.doi.org/10.1038/nmicrobiol.2016.172.
Full Text & Related Files:
Abstract: Multi-protein complexes organized by cytoskeletal proteins are essential for cell wall biogenesis in most bacteria. Current models of the wall assembly mechanism assume class A penicillin-binding proteins (aPBPs), the targets of penicillin-like drugs, function as the primary cell wall polymerases within these machineries. Here, we use an in vivo cell wall polymerase assay in Escherichia coli combined with measurements of the localization dynamics of synthesis proteins to investigate this hypothesis. We find that aPBP activity is not necessary for glycan polymerization by the cell elongation machinery as is commonly believed. Instead, our results indicate that cell wall synthesis is mediated by two distinct polymerase systems, SEDS-family proteins working within the cytoskeletal machines and aPBP enzymes functioning outside of these complexes. These findings thus necessitate a fundamental change in our conception of the cell wall assembly process in bacteria.
Published Version: doi:10.1038/nmicrobiol.2016.172
Other Sources: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5030067/pdf/
Terms of Use: This article is made available under the terms and conditions applicable to Other Posted Material, as set forth at http://nrs.harvard.edu/urn-3:HUL.InstRepos:dash.current.terms-of-use#LAA
Citable link to this page: http://nrs.harvard.edu/urn-3:HUL.InstRepos:32072123
Downloads of this work:

Show full Dublin Core record

This item appears in the following Collection(s)

 
 

Search DASH


Advanced Search
 
 

Submitters