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铜绿假单胞菌 PA1006 是一种经过硫化物修饰的蛋白质，对钼的动态平衡至关重要。

Pseudomonas aeruginosa PA1006 is a persulfide-modified protein that is critical for molybdenum homeostasis.

机构信息

Department of Microbiology and Immunology, University of Rochester School of Medicine and Dentistry, Rochester, New York, USA.

出版信息

PLoS One. 2013;8(2):e55593. doi: 10.1371/journal.pone.0055593. Epub 2013 Feb 8.

DOI:10.1371/journal.pone.0055593
PMID:23409003
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3568144/
Abstract

A companion manuscript revealed that deletion of the Pseudomonas aeruginosa (Pae) PA1006 gene caused pleiotropic defects in metabolism including a loss of all nitrate reductase activities, biofilm maturation, and virulence. Herein, several complementary approaches indicate that PA1006 protein serves as a persulfide-modified protein that is critical for molybdenum homeostasis in Pae. Mutation of a highly conserved Cys22 to Ala or Ser resulted in a loss of PA1006 activity. Yeast-two-hybrid and a green-fluorescent protein fragment complementation assay (GFP-PFCA) in Pae itself revealed that PA1006 interacts with Pae PA3667/CsdA and PA3814/IscS Cys desulfurase enzymes. Fourier transform ion cyclotron resonance mass spectrometry (FT-ICR-MS) "top-down" analysis of PA1006 purified from Pae revealed that conserved Cys22 is post-translationally modified in vivo in the form a persulfide. Inductively-coupled-plasma (ICP)-MS analysis of ΔPA1006 mutant extracts revealed that the mutant cells contain significantly reduced levels of molybdenum compared to wild-type. GFP-PFCA also revealed that PA1006 interacts with several molybdenum cofactor (MoCo) biosynthesis proteins as well as nitrate reductase maturation factor NarJ and component NarH. These data indicate that a loss of PA1006 protein's persulfide sulfur and a reduced availability of molybdenum contribute to the phenotype of a ΔPA1006 mutant.

摘要

一篇相关的论文阐明，敲除铜绿假单胞菌（Pseudomonas aeruginosa，Pae）PA1006 基因导致代谢的多种缺陷，包括丧失所有硝酸盐还原酶活性、生物膜成熟和毒力。在此，几种互补的方法表明，PA1006 蛋白作为一种硫代修饰蛋白，对 Pae 中的钼稳态至关重要。将高度保守的 Cys22 突变为丙氨酸或丝氨酸，会导致 PA1006 活性丧失。酵母双杂交和 Pae 自身的绿色荧光蛋白片段互补分析（GFP-PFCA）表明，PA1006 与 Pae PA3667/CsdA 和 PA3814/IscS 半胱氨酸脱硫酶相互作用。从 Pae 中纯化的 PA1006 的傅里叶变换离子回旋共振质谱（FT-ICR-MS）“自上而下”分析表明，保守的 Cys22 在体内以硫代修饰的形式发生翻译后修饰。对ΔPA1006 突变体提取物的电感耦合等离子体质谱（ICP-MS）分析表明，与野生型相比，突变细胞中的钼含量显著降低。GFP-PFCA 还表明，PA1006 与几种钼辅因子（MoCo）生物合成蛋白以及硝酸盐还原酶成熟因子 NarJ 和组成部分 NarH 相互作用。这些数据表明，PA1006 蛋白的硫代修饰硫和钼可用性的减少导致了ΔPA1006 突变体的表型。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/895c/3568144/e948cb8482e0/pone.0055593.g008.jpg
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