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J. Biol. Chem., Vol. 281, Issue 37, 26985-26993, September 15, 2006

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In Vitro Synthesis of Cross-linked Murein and Its Attachment to Sacculi by PBP1A from Escherichia coli^*

Petra Born, Eefjan Breukink, and Waldemar Vollmer¹

From the Mikrobielle Genetik, Universität Tübingen, Auf der Morgenstelle 28, 72076 Tübingen, Germany and Center of Biomembranes and Lipid Enzymology, Department of Biochemistry of Membranes, Institute for Biomembranes, University of Utrecht, Padualaan 8, 3584 CH Utrecht, The Netherlands

The penicillin-binding protein (PBP) 1A is a major murein (peptidoglycan) synthase in Escherichia coli. The murein synthesis activity of PBP1A was studied in vitro with radioactive lipid II substrate. PBP1A produced murein glycan strands by transglycosylation and formed peptide cross-links by transpeptidation. Time course experiments revealed that PBP1A, unlike PBP1B, required the presence of polymerized glycan strands carrying monomeric peptides for cross-linking activity. PBP1A was capable of attaching nascent murein synthesized from radioactive lipid II to nonlabeled murein sacculi. The attachment of the new material occurred by transpeptidation reactions in which monomeric triand tetrapeptides in the sacculi were the acceptors.

Received for publication, April 28, 2006 , and in revised form, June 12, 2006.

^* This project was supported by the Deutsche Forschungsgemeinschaft within the Forschergruppe Bakterielle Zellhülle (FOR 449) and by the European Commission EUR-INTAFAR (LSHM-CT-2004-512138) network. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ To whom correspondence should be addressed: Microbial Genetics, University of Tübingen, Auf der Morgenstelle 28, 72076 Tübingen, Germany. Tel.: 49-7071-2974635; Fax: 49-7071-295065; E-mail: waldemar.vollmer{at}uni-tuebingen.de.

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