The Soluble Periplasmic Domains of Escherichia coli Cell Division Proteins FtsQ/FtsB/FtsL Form a Trimeric Complex with Submicromolar Affinity
Autor: | Glas, Marjolein, Bart Van Den Berg Van Saparoea, H., McLaughlin, Stephen H., Roseboom, Winfried, Liu, Fan, Koningstein, Gregory M., Fish, Alexander, Den Blaauwen, Tanneke, Heck, Albert J R, De Jong, Luitzen, Bitter, Wilbert, De Esch, Iwan J P, Luirink, Joen, Biomolecular Mass Spectrometry and Proteomics, Sub Biomol.Mass Spectrometry & Proteom., Sub Biomol.Mass Spect. and Proteomics |
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Přispěvatelé: | Medical Microbiology and Infection Prevention, CCA - Immuno-pathogenesis, Biomolecular Mass Spectrometry and Proteomics, Sub Biomol.Mass Spectrometry & Proteom., Sub Biomol.Mass Spect. and Proteomics, Molecular Microbiology, Medicinal chemistry, AIMMS, LaserLaB - Analytical Chemistry and Spectroscopy, Theoretical Life Sciences, Mass Spectrometry of Biomacromolecules (SILS, FNWI), Bacterial Cell Biology & Physiology (SILS, FNWI), Systems Biology |
Jazyk: | angličtina |
Rok vydání: | 2015 |
Předmět: |
Models
Molecular Cell division Light Molecular Sequence Data Cell Cycle Proteins Biosensing Techniques Biology medicine.disease_cause Microbiology Biochemistry Mass Spectrometry FtsQBL complex Protein–protein interaction Structure-Activity Relationship TheoryofComputation_ANALYSISOFALGORITHMSANDPROBLEMCOMPLEXITY ComputingMethodologies_SYMBOLICANDALGEBRAICMANIPULATION parasitic diseases medicine Escherichia coli Inner membrane Amino Acid Sequence Molecular Biology C-terminus Escherichia coli Proteins Membrane Proteins Periplasmic space Cell Biology Cell biology Protein Structure Tertiary Molecular Weight Protein Subunits Cross-Linking Reagents Immobilized Proteins Solubility Multiprotein Complexes Periplasm Bacterial outer membrane Peptides Ultracentrifugation Cell Division Protein Binding MathematicsofComputing_DISCRETEMATHEMATICS |
Zdroj: | Journal of Biological Chemistry, 290(35), 21498-21509. American Society for Biochemistry and Molecular Biology Inc. The Journal of Biological Chemistry, 290(35), 21498-21509. American Society for Biochemistry and Molecular Biology Inc. Glas, M, van den Berg van Saparoea, H B, Mclaughlin, S H, Roseboom, W, Liu, F, Koningstein, G M, Fish, A, den Blaauwen, T, Heck, A J, de Jong, L D, Bitter, W, de Esch, I J P & Luirink, S 2015, ' The Soluble Periplasmic Domains of Escherichia coli Cell Division Proteins FtsQ/FtsB/FtsL Form a Trimeric Complex with Submicromolar Affinity. ', Journal of Biological Chemistry, vol. 290, no. 35, pp. 21498-21509 . https://doi.org/10.1074/jbc.M115.654756 Journal of Biological Chemistry, 290(35), 21498. American Society for Biochemistry and Molecular Biology Inc. |
ISSN: | 0021-9258 |
Popis: | Cell division in Escherichia coli involves a set of essential proteins that assembles at midcell to form the so-called divisome. The divisome regulates the invagination of the inner membrane, cell wall synthesis, and inward growth of the outer membrane. One of the divisome proteins, FtsQ, plays a central but enigmatic role in cell division. This protein associates with FtsB and FtsL, which, like FtsQ, are bitopic inner membrane proteins with a large periplasmic domain (denoted FtsQp, FtsBp, and FtsLp) that is indispensable for the function of each protein. Considering the vital nature and accessible location of the FtsQBL complex, it is an attractive target for protein-protein interaction inhibitors intended to block bacterial cell division. In this study, we expressed FtsQp, FtsBp, and FtsLp individually and in combination. Upon co-expression, FtsQp was co-purified with FtsBp and FtsLp from E. coli extracts as a stable trimeric complex. FtsBp was also shown to interact with FtsQp in the absence of FtsLp albeit with lower affinity. Interactions were mapped at the C terminus of the respective domains by site-specific cross-linking. The binding affinity and 1:1:1 stoichiometry of the FtsQpBpLp complex and the FtsQpBp subcomplex were determined in complementary surface plasmon resonance, analytical ultracentrifugation, and native mass spectrometry experiments. |
Databáze: | OpenAIRE |
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