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Both affinity chromatography and immunoprecipitation approaches demonstrated the existence of multienzyme complexes in Caulobacter crescentus membranes involving PBP1a, -2, and -3a and the morphogenic protein MreC ( 7, 9). Affinity chromatography was also used to indicate that membrane-bound LT A (MltA) interacts with PBP2 in Neisseria meningitidis serogroup B ( 15). With Escherichia coli, a protein-protein interaction network between high-molecular-weight (HMW) PBPs, HMW LTs, and low-molecular-weight PBPs (specifically, d,d-endopeptidases) has been demonstrated by affinity chromatography experiments ( 3, 26, 34, 35). Support for this hypothesis is confined to only a few studies involving a limited number of bacterial species. These conflicting enzymatic activities are thought to be controlled by the association of the respective enzymes in multienzyme complexes ( 14, 29). The lytic transglycosylases (LTs), on the other hand, cleave the β-1,4-glycosidic bond between MurNAc and GlcNAc and are understood to function as space-makers for the incorporation of new material (reviewed in reference 29). The penicillin-binding proteins (PBPs) are biosynthetic enzymes that catalyze transglycosylation and/or transpeptidation reactions for the incorporation of new material into the PG layer ( 11). Enlargement and growth of the peptidoglycan (PG) sacculus is effected by the coordination of both synthetic and lytic enzymes.