Backbone 1H, 13C and 15N assignments of the apo-acyl carrier protein (ACP1) of Pseudomonas aeruginosa

IF 0.8 4区 生物学 Q4 BIOPHYSICS
Madison Rizzo, Eric Baggs, Abu Sayeed Chowdhury, Rajesh Nagarajan, Lisa Rose Warner
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引用次数: 0

Abstract

The N-acyl-L-homoserine lactone (AHL) quorum sensing regulates virulence in the opportunistic pathogen, Pseudomonas aeruginosa. The LasI and RhlI AHL synthases use acyl carrier protein substrates to synthesize, respectively, the 3-oxododecanoyl-L-homoserine lactone (3-oxoC12-HSL) and butyryl-L-homoserine lactone (C4-HSL) QS signals for this bacterium. Although P. aeruginosa genome contains three open reading frames to encode three acyl carrier proteins, namely the ACP1, ACP2 and ACP3, microarray and gene replacement studies show that only the ACP1 carrier protein is under quorum sensing regulation. In this study, we isotopically enriched one of the acyl carrier proteins, ACP1 from P. aeruginosa and describe the backbone resonance assignments for this protein to delineate the structural and molecular basis of ACP1 recognition in P. aeruginosa AHL quorum sensing signal synthesis.

Abstract Image

铜绿假单胞菌载脂蛋白载体蛋白(ACP1)骨架1H, 13C和15N的分配
N-酰基-L-丝氨酸内酯(AHL)群体感应调节机会性病原体铜绿假单胞菌的毒力。LasI和RhlI-AHL合成酶使用酰基载体蛋白底物分别合成该细菌的3-氧代十二烷酰基-L-高丝氨酸内酯(3-氧代C12-HSL)和丁酰基-L-高丝氨酸内酯(C4-HSL)QS信号。尽管铜绿假单胞菌基因组包含三个开放阅读框来编码三种酰基载体蛋白,即ACP1、ACP2和ACP3,但微阵列和基因替换研究表明,只有ACP1载体蛋白处于群体感应调控之下。在本研究中,我们同位素富集了来自铜绿假单胞菌的酰基载体蛋白之一ACP1,并描述了该蛋白的骨架共振分配,以描述ACP1在铜绿假单胞杆菌AHL群体感应信号合成中识别的结构和分子基础。
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来源期刊
Biomolecular NMR Assignments
Biomolecular NMR Assignments 生物-光谱学
CiteScore
1.70
自引率
11.10%
发文量
59
审稿时长
6-12 weeks
期刊介绍: Biomolecular NMR Assignments provides a forum for publishing sequence-specific resonance assignments for proteins and nucleic acids as Assignment Notes. Chemical shifts for NMR-active nuclei in macromolecules contain detailed information on molecular conformation and properties. Publication of resonance assignments in Biomolecular NMR Assignments ensures that these data are deposited into a public database at BioMagResBank (BMRB; http://www.bmrb.wisc.edu/), where they are available to other researchers. Coverage includes proteins and nucleic acids; Assignment Notes are processed for rapid online publication and are published in biannual online editions in June and December.
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