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Class A PBPs: It is time to rethink traditional paradigms
Author(s) -
Straume Daniel,
Piechowiak Katarzyna Wiaroslawa,
Kjos Morten,
Håvarstein Leiv Sigve
Publication year - 2021
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/mmi.14714
Subject(s) - penicillin binding proteins , peptidoglycan , biology , lipid ii , glycosyltransferase , bacterial cell structure , computational biology , biochemistry , function (biology) , glycan , bacteria , cell wall , microbiology and biotechnology , enzyme , bacterial protein , genetics , gene , glycoprotein
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.