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Bacterial cells have intricate internal structures. The spatial organization of constituent molecules is critical for cell life and survival. Cardiolipin is a key structural and functional constituent of the membrane surrounding each <i>Escherichia coli</i> cell. This report shows that the structure and localization of an enzyme that catalyzes cardiolipin synthesis (ClsA) may contribute to the grouping of cardiolipin with particular proteins at bacterial cell poles.
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This page is a summary of: Cardiolipin synthase A colocalizes with cardiolipin and osmosensing transporter ProP at the poles of Escherichia coli
cells, Molecular Microbiology, January 2018, Wiley,
DOI: 10.1111/mmi.13904.
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