The essential peptidoglycan glycosyltransferase MurG forms a complex with proteins involved in lateral envelope growth as well as with proteins involved in cell division in Escherichia coli

Abstract

Summary In Escherichia coli many enzymes including MurG are directly involved in the synthesis and assembly of peptidoglycan. MurG is an essential glycosyltransferase catalysing the last intracellular step of peptidoglycan synthesis. To elucidate its role during elongation and division events, localization of MurG using immunofluorescence microscopy was performed. MurG exhibited a random distribution in the cell envelope with a relatively higher intensity at the division site. This mid‐cell localization was dependent on the presence of a mature divisome. Its localization in the lateral cell wall appeared to require the presence of MreCD. This could be indicative of a potential interaction between MurG and other proteins. Investigating this by immunoprecipitation revealed the association of MurG with MreB and MraY in the same protein complex. In view of this, the loss of rod shape of Δ mreBCD strain could be ascribed to the loss of MurG membrane localization. Consequently, this could prevent the localized supply of the lipid II precursor to the peptidoglycan synthesizing machinery involved in cell elongation. It is postulated that the involvement of MurG in the peptidoglycan synthesis concurs with two complexes, one implicated in cell elongation and the other in division. A model representing the first complex is proposed.

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Cited by papers we hold 6

• Putative hexameric glycosyltransferase functional unit revealed by the crystal structure of Acinetobacter baumannii MurG · 2021
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• The Membrane Steps of Bacterial Cell Wall Synthesis as Antibiotic Targets · 2016
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• Structural Insights into Protein-Protein Interactions Involved in Bacterial Cell Wall Biogenesis · 2016
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• Bacterial actin MreB forms antiparallel double filaments · 2014
  Corrected
• A network-based approach to identify substrate classes of bacterial glycosyltransferases · 2014
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• Portrait of a Pathogen: The Mycobacterium tuberculosis Proteome In Vivo · 2010
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