Lipid II flippases play an essential role in cell growth and the maintenance of cell shape in many rod-shaped bacteria. The putative lipid II flippase RodA is an integral membrane protein and member of the SEDS (shape, elongation, division and sporulation) protein family. In contrast to its homologues in Escherichia coli and Bacillus subtilis little is known about the role of RodA in actinobacteria. In this study, we describe the localization and function of RodA in Corynebacterium glutamicum, a rod-shaped, apically growing actinobacterium. RodA-GFP localizes exclusively at the cell poles. Surprisingly, time-lapse microscopy revealed that apical cell growth is sustained in a rodA deletion strain. However, growth rates and antibiotic susceptibility are altered. In the absence of RodA, it appears that apical growth is driven by lateral diffusion of lipid II that is likely flipped by the septal flippase, FtsW. Furthermore, we applied a previously described synthetic in vivo system in combination with FRET to identify an interaction between C. glutamicum RodA and the polar growth organizing protein DivIVA.
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Sci Adv
January 2025
Infectious Diseases Translational Research Programme and Department of Microbiology and Immunology, Yong Loo Lin School of Medicine, National University of Singapore, Singapore, Singapore.
Multidrug/oligosaccharidyl-lipid/polysaccharide (MOP) family transporters are essential in glycan synthesis, flipping lipid-linked precursors across cell membranes. Yet, how they select their substrates remains enigmatic. Here, we investigate the substrate specificity of the MOP transporters in the capsular polysaccharide (CPS) synthesis pathway in .
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January 2025
Department of Biology, Barnard College at Columbia University, 3009 Broadway, New York, NY 10023, USA.
The composition of eukaryotic membranes reflects a varied but precise amalgam of lipids. The genetic underpinning of how such diversity is achieved or maintained is surprisingly obscure, despite its clear metabolic and pathophysiological impact. The Arv1 protein is represented in all eukaryotes and was initially identified in the model eukaryote as a candidate transporter of lipids from the endoplasmic reticulum.
View Article and Find Full Text PDFRev Physiol Biochem Pharmacol
January 2025
Institute of Medical Sciences, University of Aberdeen, Aberdeen, Scotland, UK.
Cell membranes contain multiple charged lipids that bind proteins dynamically and their spatial organization on the inner/outer membrane leaflet, or in spatially localized areas has considerable biological importance. Myristoylated alanine-rich C kinase substrate (MARCKS) proteins and their roles as electrostatic switches are one example covered. Cell surface charge needs to be monitored and regulated continually and the roles of lipid flippases and scramblases and their electrical regulation also are considered.
View Article and Find Full Text PDFOpen Biol
January 2025
Rosalind Franklin Institute, Harwell Campus, Didcot, UK.
The enterobacterial common antigen (ECA) is conserved in Gram-negative bacteria of the order although its function is debated. ECA biogenesis depends on the Wzx/Wzy-dependent strategy whereby the newly synthesized lipid-linked repeat units, lipid III, are transferred across the inner membrane by the lipid III flippase WzxE. WzxE is part of the Wzx family and required in many glycan assembly systems, but an understanding of its molecular mechanism is hindered due to a lack of structural evidence.
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January 2025
Department of Biochemistry and Molecular Biology, McGovern Medical School, The University of Texas Health Science Center at Houston, Houston, TX 77030, USA.
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