Activation for Catalysis of Penicillin-Binding Protein 2a from Methicillin-ResistantStaphylococcusaureusby Bacterial Cell Wall

2005 ◽  
Vol 127 (7) ◽  
pp. 2056-2057 ◽  
Author(s):  
Cosimo Fuda ◽  
Dusan Hesek ◽  
Mijoon Lee ◽  
Ken-ichiro Morio ◽  
Thomas Nowak ◽  
...  
mBio ◽  
2021 ◽  
Author(s):  
Michelle A. Williams ◽  
Alena Aliashkevich ◽  
Elizaveta Krol ◽  
Erkin Kuru ◽  
Jacob M. Bouchier ◽  
...  

While the structure and function of the bacterial cell wall are well conserved, the mechanisms responsible for cell wall biosynthesis during elongation are variable. It is increasingly clear that rod-shaped bacteria use a diverse array of growth strategies with distinct spatial zones of cell wall biosynthesis, including lateral elongation, unipolar growth, bipolar elongation, and medial elongation.


2007 ◽  
Vol 190 (5) ◽  
pp. 1831-1834 ◽  
Author(s):  
Adeline Derouaux ◽  
Benoît Wolf ◽  
Claudine Fraipont ◽  
Eefjan Breukink ◽  
Martine Nguyen-Distèche ◽  
...  

ABSTRACT The monofunctional peptidoglycan glycosyltransferase (MtgA) catalyzes glycan chain elongation of the bacterial cell wall. Here we show that MtgA localizes at the division site of Escherichia coli cells that are deficient in PBP1b and produce a thermosensitive PBP1a and is able to interact with three constituents of the divisome, PBP3, FtsW, and FtsN, suggesting that MtgA may play a role in peptidoglycan assembly during the cell cycle in collaboration with other proteins.


2002 ◽  
Vol 22 (1-2) ◽  
pp. 209-222 ◽  
Author(s):  
Bénédicte Flambard

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