Send to

Choose Destination
J Biol Chem. 1994 Aug 26;269(34):21603-7.

Specific interaction of penicillin-binding proteins 3 and 7/8 with soluble lytic transglycosylase in Escherichia coli.

Author information

Max-Planck-Institut für Entwicklungsbiologie, Abteilung Biochemie, Tübingen, Federal Republic of Germany.


Soluble lytic transglycosylase 70 (Slt70), one of the better characterized murein hydrolases of Escherichia coli, was covalently bound to CNBr-activated Sepharose and used as a specific tool to screen for proteins showing an affinity for Slt70. Several proteins were specifically enriched by Slt-Sepharose affinity chromatography. Two of them were identified as the penicillin-binding proteins (PBP)3 and PBP7/8. Thus, the bifunctional synthase PBP3, specifically involved in septum formation, and PBP7/8, recently shown to be a DD-endopeptidase, bind to Slt70 in vitro. In addition, PBP7/8 was found not only to stabilize but also to stimulate the enzymatic activity of Slt70 by a protein-protein interaction. It is concluded that Slt70, PBP7/8, and PBP3 may form a multienzyme complex in vivo.

[Indexed for MEDLINE]
Free full text

Supplemental Content

Full text links

Icon for HighWire
Loading ...
Support Center