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J Biol Chem, Vol. 274, Issue 10, 6726-6734, March 5, 1999
From the Max-Planck-Institut für Entwicklungsbiologie,
Abteilung Biochemie, Spemannstraße 35, D-72076 Tübingen, Germany
Enlargement of the stress-bearing murein sacculus
of bacteria depends on the coordinated interaction of murein synthases
and hydrolases. To understand the mechanism of interaction of these two
classes of proteins affinity chromatography and surface plasmon resonance (SPR) studies were performed. The membrane-bound lytic transglycosylase MltA when covalently linked to CNBr-activated Sepharose specifically retained the penicillin-binding proteins (PBPs)
1B, 1C, 2, and 3 from a crude Triton X-100 membrane extract of
Escherichia coli. In the presence of periplasmic proteins
also PBP1A was specifically bound. At least five different non-PBPs showed specificity for MltA-Sepharose. The amino-terminal amino acid
sequence of one of these proteins could be obtained, and the
corresponding gene was mapped at 40 min on the E. coli
genome. This MltA-interacting
protein, named MipA, in addition binds to PBP1B, a
bifunctional murein transglycosylase/transpeptidase. SPR studies with
PBP1B immobilized to ampicillin-coated sensor chips showed an
oligomerization of PBP1B that may indicate a dimerization. Simultaneous
application of MipA and MltA onto a PBP1B sensor chip surface resulted
in the formation of a trimeric complex. The dissociation constant was
determined to be about 10
Demonstration of Molecular Interactions between the Murein
Polymerase PBP1B, the Lytic Transglycosylase MltA, and the Scaffolding
Protein MipA of Escherichia coli
6 M. The formation
of a complex between a murein polymerase (PBP1B) and a murein hydrolase
(MltA) in the presence of MipA represents a first step in a
reconstitution of the hypothetical murein-synthesizing holoenzyme,
postulated to be responsible for controlled growth of the
stress-bearing sacculus of E. coli.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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