Exploring the active site of acyl homoserine lactones-dependent transcriptional regulators with bacterial quorum sensing modulators using molecular mechanics and docking studies

2007 ◽  
Vol 26 (2) ◽  
pp. 581-590 ◽  
Author(s):  
Laurent Soulère ◽  
Marine Frezza ◽  
Yves Queneau ◽  
Alain Doutheau
2018 ◽  
Vol 122 (1) ◽  
pp. 52-62 ◽  
Author(s):  
Ana Carolina del V. Leguina ◽  
Carolina Nieto ◽  
Hipólito F. Pajot ◽  
Elisa V. Bertini ◽  
Walter Mac Cormack ◽  
...  

2012 ◽  
Vol 25 (5) ◽  
pp. 677-683 ◽  
Author(s):  
Fang Liu ◽  
Ziriu Bian ◽  
Zhenhua Jia ◽  
Qian Zhao ◽  
Shuishan Song

Many gram-negative bacteria use N-acyl-homoserine lactones (AHL) as quorum-sensing signals to coordinate their collective behaviors. Accumulating evidence indicates that plants can respond to AHL. However, little is known about the molecular mechanism of plants reacting to these bacterial signals. In this study, we show that the treatment of Arabidopsis roots with N-3-oxo-hexanoyl-homoserine lactone (3OC6-HSL) and N-3-oxo-octanoyl-homoserine lactone (3OC8-HSL) resulted in significant root elongation. The genetic analysis revealed that the T-DNA insertional mutants of gcr1, encoding a G-protein-coupled receptor GCR1, were insensitive to 3OC6-HSL or 3OC8-HSL in assays of root growth. The loss-of-function mutants of the sole canonical Gα subunit GPA1 showed no response to AHL promotion of root elongation whereas Gα gain-of-function plants overexpressing either the wild type or a constitutively active version of Arabidopsis Gα exhibited the exaggerated effect on root elongation caused by AHL. Furthermore, the expression of GCR1 and GPA1 were significantly upregulated after plants were contacted with both AHL. Taken together, our results suggest that GCR1 and GPA1 are involved in AHL-mediated elongation of Arabidopsis roots. This provides insight into the mechanism of plant responses to bacterial quorum-sensing signals.


Antioxidants ◽  
2021 ◽  
Vol 10 (2) ◽  
pp. 256
Author(s):  
Giuseppe Manco ◽  
Elena Porzio ◽  
Teresa Maria Carusone

PON1, PON2, and PON3 belong to a family of lactone hydrolyzing enzymes endowed with various substrate specificities. Among PONs, PON2 shows the highest hydrolytic activity toward many acyl-homoserine lactones (acyl-HL) involved in bacterial quorum-sensing signaling. Accordingly, defense against pathogens, such as Brevundimonas aeruginosa (B. aeruginosa), was postulated to be the principal function of PON2. However, recent findings have highlighted the importance of PON2 in oxidative stress control, inhibition of apoptosis, and the progression of various types of malignancies. This review focuses on all of these aspects of PON2.


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