Genomic and phenotypic analyses of Serratia fonticola strain GS2: a rhizobacterium isolated from sesame rhizosphere that promotes plant growth and produces N -acyl homoserine lactone

2017 ◽  
Vol 241 ◽  
pp. 158-162 ◽  
Author(s):  
Byung Kwon Jung ◽  
Abdur Rahim Khan ◽  
Sung-Jun Hong ◽  
Gun-Seok Park ◽  
Yeong-Jun Park ◽  
...  
Keyword(s):  
Plant Growth ◽  
Homoserine Lactone ◽  
Acyl Homoserine Lactone

Ochrobactrum sp. Pv2Z2 exhibits multiple traits of plant growth promotion, biodegradation and N-acyl-homoserine-lactone quorum sensing

2014 ◽  
Vol 64 (4) ◽  
pp. 1797-1806 ◽  
Author(s):  
Asma Imran ◽  
Marryam Jumma Abdulla Saadalla ◽  
Sami-Ullah Khan ◽  
Muhammad Sajjad Mirza ◽  
Kauser Abdulla Malik ◽  
...  
Keyword(s):  
Quorum Sensing ◽  
Plant Growth ◽  
Plant Growth Promotion ◽  
Growth Promotion ◽  
Homoserine Lactone ◽  
Acyl Homoserine Lactone ◽  
Multiple Traits

scholarly journals Bacterial signaling molecules of acyl-homoserine lactone type: effect on plant growth and stress resistance

2021 ◽  
Vol 53 (5) ◽  
pp. 371-386
Author(s):  
L.M. Babenko ◽  
◽  
I.V. Kosakivska ◽  
L.V. Voytenko ◽  
K.O. Romanenko ◽  
...  
Keyword(s):  
Plant Growth ◽  
Stress Resistance ◽  
Homoserine Lactone ◽  
Signaling Molecules ◽  
Acyl Homoserine Lactone ◽  
Bacterial Signaling

scholarly journals A single point mutation converts a glutaryl-7-aminocephalosporanic acid acylase into an N-acyl-homoserine lactone acylase

2021 ◽  
Author(s):  
Shereen A. Murugayah ◽  
Gary B. Evans ◽  
Joel D. A. Tyndall ◽  
Monica L. Gerth
Keyword(s):  
Single Point ◽  
Quorum Quenching ◽  
Homoserine Lactone ◽  
Site Directed Mutagenesis ◽  
Saturation Mutagenesis ◽  
Single Amino Acid ◽  
Single Point Mutation ◽  
Acyl Homoserine Lactone ◽  
Signalling Molecules ◽  
Single Amino Acid Residue

Abstract Objective To change the specificity of a glutaryl-7-aminocephalosporanic acid acylase (GCA) towards N-acyl homoserine lactones (AHLs; quorum sensing signalling molecules) by site-directed mutagenesis. Results Seven residues were identified by analysis of existing crystal structures as potential determinants of substrate specificity. Site-saturation mutagenesis libraries were created for each of the seven selected positions. High-throughput activity screening of each library identified two variants—Arg255Ala, Arg255Gly—with new activities towards N-acyl homoserine lactone substrates. Structural modelling of the Arg255Gly mutation suggests that the smaller side-chain of glycine (as compared to arginine in the wild-type enzyme) avoids a key clash with the acyl group of the N-acyl homoserine lactone substrate. Conclusions Mutation of a single amino acid residue successfully converted a GCA (with no detectable activity against AHLs) into an AHL acylase. This approach may be useful for further engineering of ‘quorum quenching’ enzymes.

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