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
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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