Literature DB >> 9158739

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

M von Rechenberg1, A Ursinus, J V Höltje.   

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.

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Year:  1996        PMID： 9158739     DOI： 10.1089/mdr.1996.2.155

Source DB:  PubMed          Journal:  Microb Drug Resist        ISSN： 1076-6294            Impact factor:   3.431


  26 in total

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Review 6.  Growth of the stress-bearing and shape-maintaining murein sacculus of Escherichia coli.

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9.  Beta-lactam antibiotics induce a lethal malfunctioning of the bacterial cell wall synthesis machinery.

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