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Journal Article

Affinity chromatography as a means to study multienzyme complexes involved in murein synthesis

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von Rechenberg,  M
Department Biochemistry, Max Planck Institute for Developmental Biology, Max Planck Society;

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Ursinus,  A       
Department Biochemistry, Max Planck Institute for Developmental Biology, Max Planck Society;

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Höltje,  J-V
Department Biochemistry, Max Planck Institute for Developmental Biology, Max Planck Society;

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Citation

von Rechenberg, M., Ursinus, A., & Höltje, J.-V. (1996). Affinity chromatography as a means to study multienzyme complexes involved in murein synthesis. Microbial Drug Resistance, 2(1), 155-157. doi:10.1089/mdr.1996.2.155.


Cite as: https://hdl.handle.net/21.11116/0000-000D-F19F-0
Abstract
The interaction of murein hydrolases and synthases was studied by affinity chromatography. The lytic transglycosylases Slt70 and MltB of E. coli were purified and covalently linked to CNBr-activated Sepharose. Membrane extracts were analyzed for proteins that interact with the immobilized murein hydrolases. Slt70-Sepharose was found to retain the PBPs 1b, 1c, 2, and 3. Likewise MltB-Sepharose enriched PBP 1b, 1c, and 3. Thus both lytic transglycosylases have an affinity for a transpeptidase, PBP2 and/or 3, as well as for the bifunctional transpeptidase/transglycosylase 1b. Interestingly, in addition, the poorly characterized PBP 1c interacts strongly with both Slt70 and MltB. It is speculated that the lytic transglycosylases assemble a multienzyme complex consisting of hydrolases and synthases, which is involved in growth of the stress-bearing murein sacculus.