Timing of TolA and TolQ Recruitment at the Septum Depends on the Functionality of the Tol-Pal System |
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| Affiliation: | 1. Department of Pharmacology, Vanderbilt University, Nashville, TN 37232-0146, United States;2. BioCAT, Department of Physics, Illinois Institute of Technology, Chicago, IL 60616, United States;3. Department of Biophysics, Medical College of Wisconsin, 8701 Watertown Plank Road, Milwaukee, WI 53226, United States;4. Department of Biochemistry, Vanderbilt University, Nashville, TN 37232-0146, United States;5. Division of Chemical Biology and Medicinal Chemistry, University of Texas at Austin, Austin, TX 78712, United States;6. School of Pharmacy, Sungkyunkwan University, 2066 Seobu-ro Jangan-gu, Suwon 16419, Republic of Korea;7. Center for Structural Biology, Vanderbilt University, Nashville, TN 37232-0146, United States;8. Vanderbilt Institute for Chemical Biology, Vanderbilt University, Nashville, TN 37232-0146, United States;1. CEITEC MU, Kamenice 5, 62500 Brno, Czech Republic;2. National Centre for Biomolecular Research, Faculty of Science, Masaryk University, Kamenice 5, 625 00 Brno, Czech Republic;3. Center for Interdisciplinary Biosciences, Technology and Innovation Park P.J. ?afárik University, Jesenná 5, 041 54 Ko?ice, Slovakia;4. Department of Chemistry, Faculty of Science, Masaryk University, Kamenice5, 625 00 Brno, Czech Republic;1. Centro de Biología Molecular “Severo Ochoa” (Consejo Superior de Investigaciones Científicas and Universidad Autónoma de Madrid), c/ Nicolás Cabrera 1, Campus de Cantoblanco-UAM, 28049 Madrid, Spain;2. Department of Medicinal Chemistry, Key Laboratory of Chemical Biology, Ministry of Education, School of Pharmaceutical Sciences, Cheeloo College of Medicine, Shandong University, Jinan 250012, PR China;1. IMPMC - UMR 7590 CNRS, Sorbonne Université, Muséum National d’Histoire Naturelle, Paris, France;2. RIKEN Center for Computational Science, Japan;3. Department of Physics, Graduate School of Science and Institute of Transformative Bio-Molecules, Nagoya University, Japan;4. Department of Biochemistry & Pharmacology and Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Victoria, Australia;1. Protein Structure Section, Center for Structural Biology, National Cancer Institute, Frederick, MD 21702, USA;2. Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117997, Russia |
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| Abstract: | Efficient cell division of Gram-negative bacteria requires the presence of the Tol-Pal system to coordinate outer membrane (OM) invagination with inner membrane invagination (IM) and peptidoglycan (PG) remodeling. The Tol-Pal system is a trans-envelope complex that connects the three layers of the cell envelope through an energy-dependent process. It is composed of the three IM proteins, TolA, TolQ and TolR, the periplasmic protein TolB and the OM lipoprotein Pal. The proteins of the Tol-Pal system are dynamically recruited to the cell septum during cell division. TolA, the central hub of the Tol-Pal system, has three domains: a transmembrane helix (TolA1), a long second helical periplasmic domain (TolA2) and a C-terminal globular domain (TolA3). The TolQR complex uses the PMF to energize TolA, allowing its cyclic interaction via TolA3 with the OM TolB-Pal complex. Here, we confirm that TolA2 is sufficient to address TolA to the site of constriction, whereas TolA1 is recruited by TolQ. Analysis of the protein localization as function of the bacterial cell age revealed that TolA and TolQ localize earlier at midcell in the absence of the other Tol-Pal proteins. These data suggest that TolA and TolQ are delayed from their septal recruitment by the multiple interactions of TolA with TolB-Pal in the cell envelope providing a new example of temporal regulation of proteins recruitment at the septum. |
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| Keywords: | molecular motor Tol-Pal system septum OM invagination cell division OM" },{" #name" :" keyword" ," $" :{" id" :" k0035" }," $$" :[{" #name" :" text" ," _" :" outer membrane IM" },{" #name" :" keyword" ," $" :{" id" :" k0045" }," $$" :[{" #name" :" text" ," _" :" inner membrane PG" },{" #name" :" keyword" ," $" :{" id" :" k0055" }," $$" :[{" #name" :" text" ," _" :" peptidoglycan pmf" },{" #name" :" keyword" ," $" :{" id" :" k0065" }," $$" :[{" #name" :" text" ," _" :" proton-motive force sfGFP" },{" #name" :" keyword" ," $" :{" id" :" k0075" }," $$" :[{" #name" :" text" ," _" :" super-folder green fluorescent protein |
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