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The Soluble Periplasmic Domains of E. coli Cell Division Proteins FtsQ/FtsB/FtsL form a Trimeric Complex with Sub-micromolar Affinity.

著者 Glas M , van den Berg van Saparoea HB , McLaughlin SH , Roseboom W , Liu F , Koningstein GM , Fish A , den Blaauwen T , Heck AJ , de Jong L , Bitter W , de Esch IJ , Luirink J
J Biol Chem.2015 Jul 9 ; ():.
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Cell division in E. 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 indispensible 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 (PPI) 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 FtsQpBp subcomplex were determined in complementary surface plasmon resonance, analytical ultracentrifugation and native mass spectrometry experiments.
PMID: 26160297 [PubMed - as supplied by publisher]
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