The essential peptidoglycan glycosyltransferase MurG forms a complex with proteins involved in lateral envelope growth as well as with proteins involved in cell division in Escherichia coli.

The essential peptidoglycan glycosyltransferase MurG forms a complex with proteins involved in lateral envelope growth as well as with proteins involved in cell division in Escherichia coli.
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DOI:
10.1111/j.1365-2958.2007.05851.x
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发表时间:
2007-08
影响因子:
3.6
通讯作者:
den Blaauwen T
den Blaauwen T
中科院分区:
生物学2区
文献类型:
--
作者:
Mohammadi T;Karczmarek A;Crouvoisier M;Bouhss A;Mengin-Lecreulx D;den Blaauwen T

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在大肠杆菌中,包括MurG在内的许多酶直接参与肽聚糖的合成和组装。MurG是一种必需的糖基转移酶,催化肽聚糖合成的最后一个细胞内步骤。为了阐明其在延伸和分裂事件中的作用,使用免疫荧光显微镜进行MurG的定位。MurG在细胞膜上呈随机分布,在分裂部位强度较高。这种中细胞定位依赖于成熟分裂体的存在。其在细胞侧壁中的定位似乎需要MreCD的存在。这可能表明MurG与其他蛋白质之间存在潜在的相互作用。通过免疫沉淀对此进行研究,揭示了MurG与MreB和MraY在同一蛋白质复合物中的结合。因此,ΔmreBCD菌株杆状的丧失可归因于MurG膜定位的丧失。因此,这可以防止脂质II前体向参与细胞伸长的肽聚糖合成机制的局部供应。据推测,参与MurG的肽聚糖合成同时与两个复合物,一个涉及细胞伸长和其他分裂。提出了一个代表第一复合体的模型。
In Escherichia coli many enzymes including MurG are directly involved in the synthesis and assembly of peptidoglycan. MurG is an essential glycosyltransferase catalysing the last intracellular step of peptidoglycan synthesis. To elucidate its role during elongation and division events, localization of MurG using immunofluorescence microscopy was performed. MurG exhibited a random distribution in the cell envelope with a relatively higher intensity at the division site. This mid-cell localization was dependent on the presence of a mature divisome. Its localization in the lateral cell wall appeared to require the presence of MreCD. This could be indicative of a potential interaction between MurG and other proteins. Investigating this by immunoprecipitation revealed the association of MurG with MreB and MraY in the same protein complex. In view of this, the loss of rod shape of ΔmreBCD strain could be ascribed to the loss of MurG membrane localization. Consequently, this could prevent the localized supply of the lipid II precursor to the peptidoglycan synthesizing machinery involved in cell elongation. It is postulated that the involvement of MurG in the peptidoglycan synthesis concurs with two complexes, one implicated in cell elongation and the other in division. A model representing the first complex is proposed.
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