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J Bacteriol. 2014 Aug;196(15):2889-900. doi: 10.1128/JB.01516-14. Epub 2014 Jun 2.
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本文引用的文献

1
Assembly of β-barrel proteins into bacterial outer membranes.β-桶状蛋白组装到细菌外膜中。
Biochim Biophys Acta. 2014 Aug;1843(8):1542-50. doi: 10.1016/j.bbamcr.2013.10.009. Epub 2013 Oct 14.
2
Physiological role of stalk lengthening in Caulobacter crescentus.新月柄杆菌中柄延长的生理作用。
Commun Integr Biol. 2013 Jul 1;6(4):e24561. doi: 10.4161/cib.24561. Epub 2013 Apr 12.
3
LPS unmasking of Shigella flexneri reveals preferential localisation of tagged outer membrane protease IcsP to septa and new poles.LPS 暴露出福氏志贺菌的外膜蛋白酶 IcsP 优先定位于隔膜和新极
PLoS One. 2013 Jul 25;8(7):e70508. doi: 10.1371/journal.pone.0070508. Print 2013.
4
Transcriptomic and phylogenetic analysis of a bacterial cell cycle reveals strong associations between gene co-expression and evolution.转录组和系统发育分析揭示了细菌细胞周期中基因共表达与进化之间的强关联。
BMC Genomics. 2013 Jul 5;14:450. doi: 10.1186/1471-2164-14-450.
5
Protein translocation across the inner membrane of Gram-negative bacteria: the Sec and Tat dependent protein transport pathways.革兰氏阴性菌内膜蛋白转运:Sec 和 Tat 依赖的蛋白转运途径。
Res Microbiol. 2013 Jul-Aug;164(6):505-34. doi: 10.1016/j.resmic.2013.03.016. Epub 2013 Apr 6.
6
Absence of long-range diffusion of OmpA in E. coli is not caused by its peptidoglycan binding domain.OmpA 在大肠杆菌中不存在长距离扩散,这不是由于其肽聚糖结合结构域所致。
BMC Microbiol. 2013 Mar 23;13:66. doi: 10.1186/1471-2180-13-66.
7
Biogenesis of β-barrel integral proteins of bacterial outer membrane.细菌外膜β-桶状整合蛋白的生物发生。
Biochemistry (Mosc). 2012 Nov;77(11):1221-36. doi: 10.1134/S0006297912110016.
8
General protein diffusion barriers create compartments within bacterial cells.一般蛋白质扩散屏障在细菌细胞内形成隔室。
Cell. 2012 Dec 7;151(6):1270-82. doi: 10.1016/j.cell.2012.10.046. Epub 2012 Nov 29.
9
In vivo biochemistry in bacterial cells using FRAP: insight into the translation cycle.细菌细胞内的 FRAP 生物化学:对翻译周期的深入了解。
Biophys J. 2012 Nov 7;103(9):1848-59. doi: 10.1016/j.bpj.2012.09.035.
10
Lipoproteins in bacteria: structures and biosynthetic pathways.细菌中的脂蛋白:结构与生物合成途径。
FEBS J. 2012 Dec;279(23):4247-68. doi: 10.1111/febs.12041. Epub 2012 Nov 7.

在新月柄杆菌中,外膜蛋白 OmpA2 的定位取决于基因在染色体上的位置。

Localization of the outer membrane protein OmpA2 in Caulobacter crescentus depends on the position of the gene in the chromosome.

机构信息

Instituto de Investigaciones Biomédicas, Universidad Nacional Autónoma de México, Mexico City, Mexico.

Instituto de Investigaciones Biomédicas, Universidad Nacional Autónoma de México, Mexico City, Mexico

出版信息

J Bacteriol. 2014 Aug;196(15):2889-900. doi: 10.1128/JB.01516-14. Epub 2014 Jun 2.

DOI:10.1128/JB.01516-14
PMID:24891444
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC4135674/
Abstract

The outer membrane of Gram-negative bacteria is an essential structure involved in nutrient uptake, protection against harmful substances, and cell growth. Different proteins keep the outer membrane from blebbing out by simultaneously interacting with it and with the cell wall. These proteins have been mainly studied in enterobacteria, where OmpA and the Braun and Pal lipoproteins stabilize the outer membrane. Some degree of functional redundancy exists between these proteins, since none of them is essential but the absence of two of them results in a severe phenotype. Caulobacter crescentus has a different strategy to maintain its outer membrane, since it lacks the Braun lipoprotein and Pal is essential. In this work, we characterized OmpA2, an OmpA-like protein, in this bacterium. Our results showed that this protein is required for normal stalk growth and that it plays a minor role in the stability of the outer membrane. An OmpA2 fluorescent fusion protein showed that the concentration of this protein decreases from the stalk to the new pole. This localization pattern is important for its function, and it depends on the position of the gene locus in the chromosome and, as a consequence, in the cell. This result suggests that little diffusion occurs from the moment that the gene is transcribed until the mature protein attaches to the cell wall in the periplasm. This mechanism reveals the integration of different levels of information from protein function down to genome arrangement that allows the cell to self-organize.

摘要

革兰氏阴性细菌的外膜是一种重要的结构,参与营养物质的摄取、有害物质的保护和细胞生长。不同的蛋白质通过与外膜和细胞壁同时相互作用来防止外膜起泡。这些蛋白质主要在肠杆菌中进行了研究,其中 OmpA 和 Braun 和 Pal 脂蛋白稳定外膜。这些蛋白质之间存在一定程度的功能冗余,因为它们都不是必需的,但缺少其中两种会导致严重的表型。新月形柄杆菌采用了不同的策略来维持其外膜,因为它缺乏 Braun 脂蛋白,而 Pal 是必需的。在这项工作中,我们在这种细菌中表征了 OmpA2,一种类似于 OmpA 的蛋白质。我们的结果表明,该蛋白对于正常的菌柄生长是必需的,并且在稳定外膜方面只起次要作用。OmpA2 荧光融合蛋白表明,该蛋白的浓度从菌柄到新的极点逐渐降低。这种定位模式对于其功能很重要,并且取决于基因座在染色体上的位置,进而取决于在细胞中的位置。这一结果表明,从基因转录到成熟蛋白附着在质膜中的细胞壁的那一刻起,很少有扩散发生。这种机制揭示了从蛋白质功能到基因组排列的不同层次的信息整合,使细胞能够自我组织。