arginine repressor
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2020 ◽  
Vol 1864 (7) ◽  
pp. 129597
Author(s):  
Ricardo B. Mariutti ◽  
Jorge E. Hernández-González ◽  
Andrey F.Z. Nascimento ◽  
Mariana A.B. de Morais ◽  
Mario T. Murakami ◽  
...  

2020 ◽  
Vol 6 (30) ◽  
pp. eaay9597
Author(s):  
Di Qu ◽  
Zheng Hou ◽  
Jing Li ◽  
Liyang Luo ◽  
Shan Su ◽  
...  

Staphylococcus aureus infection is difficult to eradicate because of biofilm formation and antibiotic resistance. The increasing prevalence of methicillin-resistant Staphylococcus aureus (MRSA) infection necessitates the development of a new agent against bacterial biofilms. We report a new coumarin compound, termed DCH, that effectively combats MRSA in vitro and in vivo and exhibits potent antibiofilm activity without detectable resistance. Cellular proteome analysis suggests that the molecular mechanism of action of DCH involves the arginine catabolic pathway. Using molecular docking and binding affinity assays of DCH, and comparison of the properties of wild-type and ArgR-deficient MRSA strains, we demonstrate that the arginine repressor ArgR, an essential regulator of the arginine catabolic pathway, is the target of DCH. These findings indicate that DCH is a promising lead compound and validate bacterial ArgR as a potential target in the development of new drugs against MRSA biofilms.


2016 ◽  
Vol 475 (4) ◽  
pp. 350-355 ◽  
Author(s):  
Ricardo Barros Mariutti ◽  
Anwar Ullah ◽  
Gabriela Campos Araujo ◽  
Mario Tyago Murakami ◽  
Raghuvir Krishnaswamy Arni

Author(s):  
Jina Kang ◽  
Young Woo Park ◽  
Hyun Ku Yeo ◽  
Jae Young Lee

The arginine repressor (ArgR) is a transcriptional regulator which regulates genes encoding proteins involved in arginine biosynthesis and the arginine catabolic pathway. ArgR from the alkaliphilic bacteriumBacillus haloduranswas cloned and overexpressed inEscherichia coli. ArgR (Bh2777) fromB. haloduransis composed of 149 amino-acid residues with a molecular mass of 16 836 Da. ArgR was crystallized at 296 K using 1,2-propanediol as a precipitant. Crystals of N-terminally His-tagged ArgR were obtained by the sitting-drop vapour-diffusion method. Dehydrated crystals showed a dramatic improvement in diffraction quality and diffracted to 2.35 Å resolution. The crystals belonged to the cubic space groupI23, with unit-cell parametersa=b=c= 104.68 Å. The asymmetric unit contained one monomer of ArgR, which generates a trimer by the threefold axis of the space group, giving a crystal volume per mass (VM) of 2.98 Å3 Da−1and a solvent content of 56.8%.


2014 ◽  
Vol 20 (7) ◽  
Author(s):  
Saurabh Kumar Pandey ◽  
David Řeha ◽  
Vasilina Zayats ◽  
Milan Melichercik ◽  
Jannette Carey ◽  
...  
Keyword(s):  
E Coli ◽  

2010 ◽  
Vol 192 (17) ◽  
pp. 4504-4516 ◽  
Author(s):  
Galadriel Hovel-Miner ◽  
Sebastien P. Faucher ◽  
Xavier Charpentier ◽  
Howard A. Shuman

ABSTRACT Legionella pneumophila is an intracellular pathogen that infects protozoa in aquatic environments and when inhaled by susceptible human hosts replicates in alveolar macrophages and can result in the often fatal pneumonia called Legionnaires' disease. The ability of L. pneumophila to replicate within host cells requires the establishment of a specialized compartment that evades normal phagolysosome fusion called the Legionella-containing vacuole (LCV). Elucidation of the biochemical composition of the LCV and the identification of the regulatory signals sensed during intracellular replication are inherently challenging. l-Arginine is a critical nutrient in the metabolism of both prokaryotic and eukaryotic organisms. We showed that the L. pneumophila arginine repressor homolog, ArgR, is required for maximal intracellular growth in the unicellular host Acanthamoeba castellanii. In this study, we present evidence that the concentration of l-arginine in the LCV is sensed by ArgR to produce an intracellular transcriptional response. We characterized the L. pneumophila ArgR regulon by global gene expression analysis, identified genes highly affected by ArgR, showed that ArgR repression is dependent upon the presence of l-arginine, and demonstrated that ArgR-regulated genes are derepressed during intracellular growth. Additional targets of ArgR that may account for the argR mutant's intracellular multiplication defect are discussed. These results suggest that l-arginine availability functions as a regulatory signal during Legionella intracellular growth.


2010 ◽  
Vol 6 (6) ◽  
pp. e1000801 ◽  
Author(s):  
Rebecca Strawn ◽  
Milan Melichercik ◽  
Michael Green ◽  
Thomas Stockner ◽  
Jannette Carey ◽  
...  

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