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Advanced Method for the In Vivo Measurements of Lysophospholipid Translocation Across the Inner (Cytoplasmic) Membrane of Escherichia coli.
Methods Mol Biol
December 2024
Department of Biochemistry and Molecular Biology, The University of Texas Health Science Center, McGovern Medical School, Houston, TX, USA.
Phospholipid translocation occurs ubiquitously in biological membranes and primarily is protein catalyzed. Lipid flippases mediate the net translocation of specific phospholipids from one leaflet of a membrane to the other. In the inner (cytoplasmic) membrane (IM) of Gram-negative bacteria, lysophospholipid translocase (LplT) and cytosolic bifunctional acyl-acyl carrier protein (ACP) synthetase/2-acylglycerolphosphoethanolamine acyltransferase (Aas) form a glycerophospholipid regeneration system, which is capable of facilitating rapid retrograde translocation of lyso forms of phosphatidylethanolamine (PE), phosphatidylglycerol (PG), and cardiolipin (CL) but not exogenous (host-derived) phosphatidylcholine (PC) across the IM of Gram-negative diderm (two-membraned) bacteria in consequential order lyso-PE = lyso-PG > > lysophosphatidic acid (lyso-PA) >> lyso-PC.
View Article and Find Full Text PDFInvolvement of the Cell Division Protein DamX in the Infection Process of Bacteriophage T4.
Viruses
March 2024
Institute of Biology, University of Hohenheim, 190h, Garbenstr. 30, 70599 Stuttgart, Germany.
The molecular mechanism of how the infecting DNA of bacteriophage T4 passes from the capsid through the bacterial cell wall and enters the cytoplasm is essentially unknown. After adsorption, the short tail fibers of the infecting phage extend from the baseplate and trigger the contraction of the tail sheath, leading to a puncturing of the outer membrane by the tail tip needle composed of the proteins gp5.4, gp5 and gp27.
View Article and Find Full Text PDFPreparation of Uniformly Oriented Inverted Inner (Cytoplasmic) Membrane Vesicles from Gram-Negative Bacterial Cells.
Methods Mol Biol
November 2023
Department of Biochemistry & Molecular Biology, University of Texas Health Science Center at Houston, McGovern Medical School, Houston, TX, USA.
Article Synopsis
- The study addresses the challenges of synthesizing and characterizing membrane vesicles in Gram-negative bacteria due to their complex double-membrane structure, which impacts the movement of lipids and proteins.
- Uniformly oriented inside-out (ISO) vesicles are crucial for various biochemical assays and require effective preparation methods for accurate testing.
- The paper outlines a technique for confirming the orientation of membrane vesicles by analyzing the topology of a specific E. coli protein, which helps validate the reliability of membrane preparations.
Cell Fractionation.
Methods Mol Biol
November 2023
Laboratoire d'Ingénierie des Systèmes Macromoléculaires, UMR7255, Institut de Microbiologie de la Méditerranée, Aix-Marseille Univ - CNRS, Marseille, France.
Protein function is generally dependent on its subcellular localization. In gram-negative bacteria such as Escherichia coli, a protein can be targeted to five different compartments: the cytoplasm, the inner membrane, the periplasm, the outer membrane, and the extracellular medium. Different approaches can be used to determine the protein localization within cell such as in silico identification of protein signal sequences and motifs, electron microscopy and immunogold labeling, optical fluorescence microscopy, and biochemical technics.
View Article and Find Full Text PDFA real-time analysis of protein transport via the twin arginine translocation pathway in response to different components of the protonmotive force.
J Biol Chem
November 2023
Department of Plant Biology, University of California, Davis, California, USA. Electronic address:
The twin arginine translocation (Tat) pathway transports folded protein across the cytoplasmic membrane in bacteria, archaea, and across the thylakoid membrane in plants as well as the inner membrane in some mitochondria. In plant chloroplasts, the Tat pathway utilizes the protonmotive force (PMF) to drive protein translocation. However, in bacteria, it has been shown that Tat transport depends only on the transmembrane electrical potential (Δψ) component of PMF in vitro.
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