Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review
. 2021 Jul;116(1):41-52.
doi: 10.1111/mmi.14714. Epub 2021 Mar 23.

Class A PBPs: It is time to rethink traditional paradigms

Daniel Straume  1 , Katarzyna Wiaroslawa Piechowiak  1 , Morten Kjos  1 , Leiv Sigve Håvarstein  1
Affiliations
Free article
Review

Class A PBPs: It is time to rethink traditional paradigms

Daniel Straume et al. Mol Microbiol. 2021 Jul.
Free article

Abstract

Until recently, class A penicillin-binding proteins (aPBPs) were the only enzymes known to catalyze glycan chain polymerization from lipid II in bacteria. Hence, the discovery of two novel lipid II polymerases, FtsW and RodA, raises new questions and has consequently received a lot of attention from the research community. FtsW and RodA are essential and highly conserved members of the divisome and elongasome, respectively, and work in conjunction with their cognate class B PBPs (bPBPs) to synthesize the division septum and insert new peptidoglycan into the lateral cell wall. The identification of FtsW and RodA as peptidoglycan glycosyltransferases has raised questions regarding the role of aPBPs in peptidoglycan synthesis and fundamentally changed our understanding of the process. Despite their dethronement, aPBPs are essential in most bacteria. So, what is their function? In this review, we discuss recent progress in answering this question and present our own views on the topic.

Keywords: class A PBPs; peptidoglycan synthesis; two-layered cell wall.

PubMed Disclaimer

Similar articles

See all similar articles

Cited by

See all "Cited by" articles

References

REFERENCES

    1. Alcorlo, M., Straume, D., Lutkenhaus, J., Håvarstein, L.S. & Hermoso, J.A. (2020) Structural characterization of the essential cell division protein FtsE and its interaction with FtsX in Streptococcus pneumoniae. mBio, 11, e01488-20.
    1. Arbeloa, A., Segal, H., Hugonnet, J.-E., Josseaume, N., Dubost, L., Brouard, J.-P. et al. (2004) Role of class A penicillin-binding proteins in PBP5-mediated β-lactam resistance in Enterococcus faecalis. Journal of Bacteriology, 186, 1221-1228. https://doi.org/10.1128/JB.186.5.1221-1228.2004.
    1. Banzhaf, M., van den Berg van Saparoea, B., Terrak, M., Fraipont, C., Egan, A., Philippe, J. et al. (2012) Cooperativity of peptidoglycan synthases active in bacterial cell elongation. Molecular Microbiology, 85, 179-194. https://doi.org/10.1111/j.1365-2958.2012.08103.x.
    1. Barendt, S.M., Sham, L.T. & Winkler, M.E. (2011) Characterization of mutants deficient in the L, D-carboxypeptidase (DacB) and WalRK (VicRK) regulon, involved in peptidoglycan maturation of Streptococcus pneumoniae serotype 2 strain D39. Journal of Bacteriology, 193, 2290-2300. https://doi.org/10.1128/JB.01555-10.
    1. Bartual, S.G., Straume, D., Stamsås, G.A., Muñoz, I.G., Alfonso, C., Martínez-Ripoll, M. et al. (2014) Structural basis of PcsB-mediated cell separation in Streptococcus pneumoniae. Nature Communications, 5, 3842. https://doi.org/10.1038/ncomms4842.

MeSH terms

Substances

LinkOut - more resources

-