A proteomic approach of SigX function in Pseudomonas aeruginosa outer membrane composition
A proteomic approach of SigX function in Pseudomonas aeruginosa outer membrane composition
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DOI：
10.1016/j.jprot.2013.10.022
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发表时间：
2013-12-06
影响因子：
3.3
通讯作者：
Chevalier, Sylvie
中科院分区：
文献类型：
--
作者：
Duchesne, Rachel;Bouffartigues, Emeline;Chevalier, Sylvie
SigX 是在人类机会致病菌铜绿假单胞菌基因组中预测的 19 个胞质外功能 sigma 因子之一。 SigX 参与 oprF 的转录，编码主要外膜蛋白 OprF，这是一种多效性孔蛋白，有助于维持壁结构，并且对于铜绿假单胞菌毒力至关重要。本研究旨在进一步了解 SigX 的功能。我们在这里进行了 sigX 突变体的外膜亚蛋白质组分析。蛋白质组学研究显示 8 个孔蛋白的产量较低，其中 4 个涉及铁或血红素摄取的门控通道、OprF 以及三种底物特异性蛋白 OprD、OprQ 和 OprE。另一方面，葡萄糖特异性孔蛋白 OprB 和参与 LPS 修饰的脂质 A 3-O-脱酰酶上调。我们的结果表明SigX可能参与外膜组成的控制和/或调节。生物学意义本文使用蛋白质组学方法来进一步了解铜绿假单胞菌中SigX的功能。这里提供的数据表明 SigX 参与外膜蛋白组成，并且可能与参与 OM 稳态的调节网络有关。 (C) 2013 Elsevier B.V. 保留所有权利。
SigX is one of the 19 extracytoplasmic function sigma factors that have been predicted in the human opportunistic pathogen Pseudomonas aeruginosa genome. SigX is involved in the transcription of oprF, encoding the major outer membrane protein OprF, a pleiotropic porin that contributes to the maintaining of the wall structure, and is essential to P. aeruginosa virulence. This study aimed to get further insights into the functions of SigX. We performed here an outer membrane subproteome of a sigX mutant. Proteomic investigations revealed lower production of 8 porins among which 4 gated channels involved in iron or hem uptake, OprF, and the three substrate-specific proteins OprD, OprQ and OprE. On the other side, the glucose-specific porin OprB and the lipid A 3-O-deacylase that is involved in LPS modification were up-regulated. Our results indicate that SigX may be involved in the control and/or regulation of the outer membrane composition.Biological significanceA proteomic approach was used herein to get further insights into SigX functions in P. aeruginosa. The data presented here suggest that SigX is involved in the outer membrane protein composition, and could be linked to a regulatory network involved in OM homeostasis. (C) 2013 Elsevier B.V. All rights reserved.