The lipid II flippase RodA determines morphology and growth in Corynebacterium glutamicum.

Mol Microbiol

Biocenter, Ludwig-Maximilians-University Munich, Großhaderner Straße 2-4, 82152, Planegg-Martinsried, Germany.

Published: December 2013

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.

Download full-text PDF

Source
http://dx.doi.org/10.1111/mmi.12411DOI Listing

Publication Analysis

Top Keywords

lipid flippase
8
flippase roda
8
corynebacterium glutamicum
8
cell growth
8
roda
7
growth
6
lipid
4
roda determines
4
determines morphology
4
morphology growth
4

Similar Publications

Massively parallel barcode sequencing revealed the interchangeability of capsule transporters in .

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 .

View Article and Find Full Text PDF

Arv1; a "Mover and Shaker" of Subcellular Lipids.

Contact (Thousand Oaks)

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 PDF

Membrane Surface Charge, Phospholipids, and Protein Localization.

Rev 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 PDF

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.

View Article and Find Full Text PDF

Its own architect: Flipping cardiolipin synthase.

Sci Adv

January 2025

Department of Biochemistry and Molecular Biology, McGovern Medical School, The University of Texas Health Science Center at Houston, Houston, TX 77030, USA.

Article Synopsis
  • Current understanding posits that lipid asymmetry in cell membranes is actively kept and not essential for survival, yet the inner membrane (IM) shows notable asymmetry.
  • Researchers created a specific mutant lacking phosphatidylethanolamine (PE) that relies on cardiolipin (CL) for its IM viability, uncovering how the distribution of CL is regulated in the membrane.
  • The study reveals that the enzyme ClsA adapts its structure in response to varying levels of PE, highlighting a potentially novel mechanism for sustaining lipid asymmetry in membranes without the need for specialized flippase proteins.
View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!