Peptidoglycan-associated outer membrane protein Mep45 of rumen anaerobe Selenomonas ruminantium forms a non-specific diffusion pore via its C-terminal transmembrane domain.

Peptidoglycan-associated outer membrane protein Mep45 of rumen anaerobe Selenomonas ruminantium forms a non-specific diffusion pore via its C-terminal transmembrane domain.
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DOI:
10.1080/09168451.2016.1194185
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发表时间:
2016-10
期刊:
Bioscience, biotechnology, and biochemistry
影响因子:
--
通讯作者:
Kamio Y
Kamio Y
中科院分区:
其他
文献类型:
--
作者:
Kojima S;Hayashi K;Tochigi S;Kusano T;Kaneko J;Kamio Y

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反刍月单胞菌(一种厌氧革兰氏阴性细菌)的主要外膜蛋白Mep 45包括两个不同的结构域:N-末端S-层同源(SLH)结构域,其突出到周质中并结合肽聚糖,以及剩余的C-末端跨膜结构域,其功能尚不清楚。在这里,我们溶解和纯化Mep 45,并使用Mep 45重构的蛋白脂质体表征其功能。我们发现Mep 45通过其C-末端区域形成非特异性扩散通道。该通道是可渗透的溶质小于约600的分子量,和估计的孔半径为0.58 nm。SLH结构域的截断不影响通道性质。根据Mep 45是S.反刍动物,我们得出结论,Mep 45作为一个主要途径,通过它的小溶质扩散通过该细菌的外膜。图1是S.反刍动物。Mep 45的C-末端区域形成非特异性扩散通道。
The major outer membrane protein Mep45 of Selenomonas ruminantium, an anaerobic Gram-negative bacterium, comprises two distinct domains: the N-terminal S-layer homologous (SLH) domain that protrudes into the periplasm and binds to peptidoglycan, and the remaining C-terminal transmembrane domain, whose function has been unknown. Here, we solubilized and purified Mep45 and characterized its function using proteoliposomes reconstituted with Mep45. We found that Mep45 forms a nonspecific diffusion channel via its C-terminal region. The channel was permeable to solutes smaller than a molecular weight of roughly 600, and the estimated pore radius was 0.58 nm. Truncation of the SLH domain did not affect the channel property. On the basis of the fact that Mep45 is the most abundant outer membrane protein in S. ruminantium, we conclude that Mep45 serves as a main pathway through which small solutes diffuse across the outer membrane of this bacterium. Schematic representation of Mep45 in the outer membrane of S. ruminantium. The C-terminal region of Mep45 forms a non-specific diffusion channel.
DOI: 10.1085/jgp.44.6.1189
发表时间: 1961-07
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影响因子: --
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