Feb 19, 2014

Differential localization of LTA synthesis proteins and their interaction with the cell division machinery in Staphylococcus aureus

Molecular Microbiology
Nathalie T ReichmannAngelika Gründling

Abstract

Lipoteichoic acid (LTA) is an important cell wall component of Gram-positive bacteria. In Staphylococcus aureus it consists of a polyglycerolphosphate-chain that is retained within the membrane via a glycolipid. Using an immunofluorescence approach, we show here that the LTA polymer is not surface exposed in S. aureus, as it can only be detected after digestion of the peptidoglycan layer. S. aureus mutants lacking LTA are enlarged and show aberrant positioning of septa, suggesting a link between LTA synthesis and the cell division process. Using a bacterial two-hybrid approach, we show that the three key LTA synthesis proteins, YpfP and LtaA, involved in glycolipid production, and LtaS, required for LTA backbone synthesis, interact with one another. All three proteins also interacted with numerous cell division and peptidoglycan synthesis proteins, suggesting the formation of a multi-enzyme complex and providing further evidence for the co-ordination of these processes. When assessed by fluorescence microscopy, YpfP and LtaA fluorescent protein fusions localized to the membrane while the LtaS enzyme accumulated at the cell division site. These data support a model whereby LTA backbone synthesis proceeds in S. aureus at the divi...Continue Reading

Mentioned in this Paper

Gram-Positive Bacteria
Establishment and Maintenance of Localization
Immunofluorescence Assay
Bacterial Proteins
Septa
Cell Cycle Proteins
Chimeric Proteins, Recombinant
Membrane
L-allo-threonine Aldolase Activity
Cell Division

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