Heterogeneous localisation of membrane proteins in Staphylococcus aureus

Scientific Reports
Felix WeihsSimon J Foster

Abstract

The bacterial cytoplasmic membrane is the interface between the cell and its environment, with multiple membrane proteins serving its many functions. However, how these proteins are organised to permit optimal physiological processes is largely unknown. Based on our initial findings that 2 phospholipid biosynthetic enzymes (PlsY and CdsA) localise heterogeneously in the membrane of the bacterium Staphylococcus aureus, we have analysed the localisation of other key membrane proteins. A range of protein fusions were constructed and used in conjunction with quantitative image analysis. Enzymes involved in phospholipid biosynthesis as well as the lipid raft marker FloT exhibited a heterogeneous localisation pattern. However, the secretion associated SecY protein, was more homogeneously distributed in the membrane. A FRET-based system also identified novel colocalisation between phospholipid biosynthesis enzymes and the respiratory protein CydB revealing a likely larger network of partners. PlsY localisation was found to be dose dependent but not to be affected by membrane lipid composition. Disruption of the activity of the essential cell division organiser FtsZ, using the inhibitor PC190723 led to loss of PlsY localisation, reveal...Continue Reading

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Citations

Dec 13, 2019·Biochemical Society Transactions·Paul Richard Jesena Yulo, Heather Lyn Hendrickson
Nov 26, 2020·Nature Communications·Christopher B MulhollandHeinrich Leonhardt

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Methods Mentioned

BETA
Fluorescence
fluorescence microscopy
FRET

Software Mentioned

SecY
GraphPad Prism
NIS elements
ImageJ
NanoJ
Fiji
Softworx
PlsY
Fiji ImageJ
- SRRF

Related Concepts

Related Papers

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