The Soluble Periplasmic Domains of Escherichia coli Cell Division Proteins FtsQ/FtsB/FtsL Form a Trimeric Complex with Submicromolar Affinity.

M. Glas, H.B. van den Berg van Saparoea, S.H. Mclaughlin, W. Roseboom, F. Liu, G.M. Koningstein, A. Fish, T. den Blaauwen, A.J. Heck, L. de de Jong, W. Bitter, I.J.P. de Esch, S. Luirink

Research output: Contribution to JournalArticleAcademicpeer-review

Abstract

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 FtsQ<inf>p</inf>, FtsB<inf>p</inf>, and FtsL<inf>p</inf>) 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 FtsQ<inf>p</inf>, FtsB<inf>p</inf>, and FtsL<inf>p</inf> individually and in combination. Upon co-expression, FtsQ<inf>p</inf> was co-purified with FtsB<inf>p</inf> and FtsL<inf>p</inf> from E. coli extracts as a stable trimeric complex. FtsB<inf>p</inf> was also shown to interact with FtsQ<inf>p</inf> in the absence of FtsL<inf>p</inf> 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 FtsQ<inf>p</inf>B<inf>p</inf>L<inf>p</inf> complex and the FtsQ<inf>p</inf>B<inf>p</inf> subcomplex were determined in complementary surface plasmon resonance, analytical ultracentrifugation, and native mass spectrometry experiments.
Original languageEnglish
Pages (from-to)21498-21509
JournalJournal of Biological Chemistry
Volume290
Issue number35
DOIs
Publication statusPublished - 2015

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