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Journal ArticleDOI

On the role of the high molecular weight penicillin-binding proteins in the cell cycle of Escherichia coli.

Frans B. Wientjes, +1 more
- 01 Jan 1991 - 
- Vol. 142, pp 333-344
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TLDR
It was suggested that PBP1A/1B do not have a specific function in either elongation or constriction, rather, they seem to have a general activity on the basis of which the other synthesizing PBP perform their special tasks.
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This article is published in Research in Microbiology.The article was published on 1991-01-01. It has received 80 citations till now. The article focuses on the topics: Peptidoglycan & Penicillin binding proteins.

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Citations
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Journal ArticleDOI

Growth of the Stress-Bearing and Shape-Maintaining Murein Sacculus of Escherichia coli

TL;DR: A model is presented that postulates that maintenance of bacterial shape is achieved by the enzyme complex copying the preexisting murein sacculus that plays the role of a template.
Journal ArticleDOI

Formation of the glycan chains in the synthesis of bacterial peptidoglycan

TL;DR: The aim of the present review is to summarize and evaluate the molecular and cellullar data concerning the formation of the glycan chains in the synthesis of peptidoglycan, which is an interesting target for antibacterials.
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Diverse Paths to Midcell: Assembly of the Bacterial Cell Division Machinery

TL;DR: There is evidence for a complex web of interactions among these proteins and at least one distinct subcomplex of cell division proteins has been defined, which is conserved among E. coli, Bacillus subtilis and Streptococcus pneumoniae.
Journal ArticleDOI

Chromosome and Low Copy Plasmid Segregation in E. coli: Visual Evidence for Distinct Mechanisms

TL;DR: This analysis suggests that different active processes are involved in movement and localization of the chromosome and of the two plasmids during segregation.
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The bacterial actin MreB rotates, and rotation depends on cell-wall assembly

TL;DR: It is shown that MreB rotates around the long axis of the cell in a persistent manner and does not depend on its own polymerization but rather requires the assembly of the peptidoglycan cell wall, expanding the view of cytoskeletal motors and deepening the understanding of the physical basis of bacterial morphogenesis.
References
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Journal Article

Protein Measurement with the Folin Phenol Reagent

TL;DR: Procedures are described for measuring protein in solution or after precipitation with acids or other agents, and for the determination of as little as 0.2 gamma of protein.
Journal ArticleDOI

Distinct penicillin binding proteins involved in the division, elongation, and shape of Escherichia coli K12.

TL;DR: Evidence is presented that penicillin bulge formation is due to the inhibition of proteins 2 and 3 in the absence of inhibition of protein 1.
Journal ArticleDOI

Penicillin-binding proteins and cell shape in E. coli

TL;DR: The identification of a minor penicillin binding protein is reported which is believed to be the target at which the amidinopenicillanic acid designated FL1060 acts to affect the shape of Escherichia coli.
Journal ArticleDOI

Autolytic enzymes and cell division of Escherichia coli.

TL;DR: By localizing the site of action of murein hydrolases which are directly involved in bacterial morphogenesis, this structural element of the cell wall is enlarged exactly as predicted by the replicon hypothesis.
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