iTRAQ-based quantitative proteomic analysis of Pseudomonas aeruginosa SJTD-1: A global response to n-octadecane induced stress

iTRAQ-based quantitative proteomic analysis of Pseudomonas aeruginosa SJTD-1: A global response to n-octadecane induced stress
复制标题

基于 iTRAQ 的铜绿假单胞菌 SJTD-1 定量蛋白质组学分析:对正十八烷诱导应激的整体反应

DOI:
10.1016/j.jprot.2015.03.034
复制
发表时间:
2015-06-18
影响因子:
3.3
通讯作者:
Liu, Jian-Hua
Liu, Jian-Hua
中科院分区:
生物学2区
文献类型:
--
作者:
Liu, Huan;Sun, Wen-Bing;Liu, Jian-Hua

文献摘要

被引文献

相似文献

铜绿假单胞菌SJTD-1能有效地消耗最短的固态烷烃正十八烷。为了揭示其机制,应用iTRAQ-LC-MS/MS策略定量蛋白质对烷烃的响应。结果,共鉴定出383个烷烃响应蛋白,这些蛋白可能与多种生化途径有关。烷烃羟化酶AlkB 2在烷烃条件下的表达水平明显高于其它条件下。首次提出了假单胞菌中存在一种新的AlmA-like单加氧酶及其在烷烃羟基化反应中的作用。此外,用于趋化、β-氧化、乙醛酸旁路、烷烃摄取、跨膜转运、酶促步骤和碳流的其他蛋白质可能在细胞对烷烃的反应中具有重要作用。这些差异表达的蛋白质中的大多数在功能上被映射到烷烃降解或其代谢的途径中。因此,本研究的结果为揭示长链烷烃的生物降解提供了重要线索,并为今后开发高效的生物催化剂提供了重要的理论依据。生物学意义首次采用iTRAQ策略比较了假单胞菌SJTD-1降解烷烃的蛋白质组。蛋白质的变化清楚地提供了关于SJTD-1的烷烃羟基化的全面概述,包括那些用于趋化性、烷烃摄取、跨膜转运、酶促步骤和碳流的蛋白质。AlkB 2和一种新的AlmA-like单加氧酶对烷烃的应用有着重要的贡献。我们发现,几个趋化性蛋白质改变了丰富的烷烃生长的细胞。这些结果可能有助于理解烷烃的假单胞菌使用。(C)2015年由Elsevier B. V.出版
N-octadecane, the shortest solid-state alkane, was efficiently consumed by Pseudomonas aeruginosa SJTD-1. To reveal its mechanism, the iTRAQ-LC-MS/MS strategy was applied for quantification of proteins in response to alkane. As a result, 383 alkane-responsive proteins were identified and these proteins could be linked to multiple biochemical pathways. Above all, the level of alkane hydroxylase AlkB2 has been significantly higher in alkane condition. Also, the presence of a putative novel AlmA-like monooxygenase and its role on alkane hydroxylation were firstly proposed in Pseudorrionas. In addition, other proteins for chemotaxic, beta-oxidation, glyoxylate bypass, alkane uptake, cross membrane transport, enzymatic steps and the carbon flow may have important roles in the cellular response to alkane. Most of those differently expressed proteins were functionally mapped into pathways of alkane degradation or metabolism thereof. In this sense, findings in this study provide critical clues to reveal biodegradation of long chain n-alkanes and rationally be important for potent biocatalyst for bioremediation in future.Biological significanceWe use iTRAQ strategy firstly to compare the proteomes of Pseudomonas SJTD-1 degrading alkane. Changes in protein clearly provide a comprehensive overview on alkane hydroxylation of SJTD-1, including those proteins for chemotaxis, alkane uptake, cross membrane transport, enzymatic steps and the carbon flow. AlkB2 and a putative novel AlmA-like monooxygenase have been highlighted for their outstanding contribution to alkane use. We found that several chemotaxic proteins were altered in abundance in alkane-grown cells. These results may be helpful for understanding alkane use for Pseudomonas. (C) 2015 Published by Elsevier B.V.