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

被引：59

作者：

vonRechenberg, M ^{[1
]}

Ursinus, A ^{[1
]}

Holtje, JV ^{[1
]}

机构：

[1] MAX PLANCK INST ENTWICKLUNGSBIOL, D-72076 TUBINGEN, GERMANY

来源：

MICROBIAL DRUG RESISTANCE | 1996年 / 2卷 / 01期

关键词：

D O I：

10.1089/mdr.1996.2.155

中图分类号：

R51 [传染病];

学科分类号：

100401 ;

摘要：

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 Ib, Ic, 2, and 3, Likewise MltB-Sepharose enriched PBP Ib, Ic, and 3, Thus both lytic transglycosylases have an affinity for a transpeptidase, PBP2 and/or 3, as well as for the bifunctional transpeptidase/transglycosylase Ib, Interestingly, in addition, the poorly characterized PBP Ic 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.

引用

页码：155 / 157

页数：3

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