Complete genome sequence and characterization of the N-acylhomoserine lactone-degrading gene of the potato leaf-associated Solibacillus silvestris

Morohoshi, Toshio; Tominaga, Yoshiaki; Someya, Nobutaka; Ikeda, Tsukasa

doi:10.1016/j.jbiosc.2011.09.006

Cited by 50 publications

(28 citation statements)

References 28 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…AiiAtype AHL lactonases, which belong to the metallo-␤-lactamase superfamily, have been identified and characterized from various bacteria (8,9,14,17,22,29). However, AidC has less than 13% identity to each of the known AiiA-type AHL lactonases, including 13% identity across the entire length of AiiA from Bacillus sp.…”

Section: Resultsmentioning

confidence: 99%

“…240B1, 12% identity across AttM from Agrobacterium tumefaciens strain C58 (29) and AhlD from Arthrobacter sp. strain IBN110 (15), 10% identity across AhlS from Solibacillus silvestris strain StLB046 (14), and 8% identity across QlcA from the soil metagenome (17). When the amino acid sequence of AidC was compared with those of the known AiiA-type lactonases (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…4). Interestingly, D191 of AiiA, which has been proven to be essential for enzymatic activity by site-directed mutagenesis (8) and is shared by all the known AiiA-type lactonases (8,14,15,17,29), was replaced by L261 in AidC (Fig. 4).…”

Section: Resultsmentioning

confidence: 99%

See 2 more Smart Citations

AidC, a Novel N -Acylhomoserine Lactonase from the Potato Root-Associated Cytophaga-Flavobacteria-Bacteroides (CFB) Group Bacterium Chryseobacterium sp. Strain StRB126

Wang

Morohoshi

Someya

et al. 2012

Appl Environ Microbiol

Self Cite

View full text Add to dashboard Cite

b N-Acylhomoserine lactones (AHLs) are used as quorum-sensing (QS) signal molecules by many Gram-negative bacteria. We have reported that Chryseobacterium sp. strain StRB126, which was isolated from the root surface of potato, has AHL-degrading activity. In this study, we cloned and characterized the aidC gene from the genomic library of StRB126. AidC has AHL-degrading activity and shows homology to several metallo-␤-lactamase proteins from Bacteroidetes, although not to any known AHL-degrading enzymes. Purified AidC, as a maltose-binding fusion protein, showed high degrading activity against all tested AHLs, whether short-or long-chain forms, with or without substitution at carbon 3. High-performance liquid chromatography (HPLC) analysis revealed that AidC functions as an AHL lactonase catalyzing AHL ring opening by hydrolyzing lactones. An assay to determine the effects of covalent and ionic bonding showed that Zn 2؉ is important to AidC activity both in vitro and in vivo. In addition, the aidC gene could also be PCR amplified from several other Chryseobacterium strains. In conclusion, this study indicated that the aidC gene, encoding a novel AHL lactonase, may be widespread throughout the genus Chryseobacterium. Our results extend the diversity and known bacterial hosts of AHL-degrading enzymes.

show abstract

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

AidC, a Novel N -Acylhomoserine Lactonase from the Potato Root-Associated Cytophaga-Flavobacteria-Bacteroides (CFB) Group Bacterium Chryseobacterium sp. Strain StRB126

Wang

Morohoshi

Someya

et al. 2012

Appl Environ Microbiol

Self Cite

View full text Add to dashboard Cite

show abstract

“…The amiE-coding region on the Ooi24 genome was amplified with Blend Taq DNA polymerase and the primers 5=-TCT AAG CTT CCG ATC ATG AGC TTC AAT ATT GCA CC-3= and 5=-TCT GGA TCC TCG TCA ATC AAT TGA TTT CTA GTC GG-3= containing the HindIII and (23). The plasmids pBBR1MCS5, pBBR1-amiE, and pBBR1-ahlS were transformed into P. aeruginosa PAO1 via electroporation (24).…”

Section: Methodsmentioning

confidence: 99%

AmiE, a Novel N -Acylhomoserine Lactone Acylase Belonging to the Amidase Family, from the Activated-Sludge Isolate Acinetobacter sp. Strain Ooi24

Ochiai

Yasumoto

Morohoshi

et al. 2014

Appl Environ Microbiol

Self Cite

View full text Add to dashboard Cite

Many Gram-negative bacteria use N-acyl-L-homoserine lactones (AHLs) as quorum-sensing signal molecules. We have reported that Acinetobacter strains isolated from activated sludge have AHL-degrading activity. In this study, we cloned the amiE gene as an AHL-degradative gene from the genomic library of Acinetobacter sp. strain Ooi24. High-performance liquid chromatography analysis revealed that AmiE functions as an AHL acylase, which hydrolyzes the amide bond of AHL. AmiE showed a high level of degrading activity against AHLs with long acyl chains but no activity against AHLs with acyl chains shorter than eight carbons. AmiE showed homology with a member of the amidases (EC 3.5.1.4) but not with any known AHL acylase enzymes. An amino acid sequence of AmiE from Ooi24 showed greater than 99% identities with uncharacterized proteins from Acinetobacter ursingii CIP 107286 and Acinetobacter sp. strain CIP 102129, but it was not found in the draft or complete genome sequences of other Acinetobacter strains. The presence of transposase-like genes around the amiE genes of these three Acinetobacter strains suggests that amiE is transferred by a putative transposon. Furthermore, the expression of AmiE in Pseudomonas aeruginosa PAO1 reduced AHL accumulation and elastase activity, which were regulated by AHL-mediated quorum sensing.

show abstract

“…The PCR products were digested with XbaI and BamHI and then inserted into the XbaI-BamHI site of pMAL-c2X to construct pMAL-aiiA. The construction of the pMAL-ahlS and pMALaidC plasmids, which express the MBP-AhlS and MBP-AidC fusion proteins, respectively, were described in previous studies (5,6).…”

Section: Purification Of Ahl Lactonases As Maltose Binding Protein Fumentioning

confidence: 99%

Characterization of a novel thermostable N-acylhomoserine lactonase from the thermophilic bacterium Thermaerobacter marianensis

Morohoshi

Tominaga

Someya

et al. 2015

Journal of Bioscience and Bioengineering

Self Cite

View full text Add to dashboard Cite

Complete genome sequence and characterization of the N-acylhomoserine lactone-degrading gene of the potato leaf-associated Solibacillus silvestris

Cited by 50 publications

References 28 publications

AidC, a Novel N -Acylhomoserine Lactonase from the Potato Root-Associated Cytophaga-Flavobacteria-Bacteroides (CFB) Group Bacterium Chryseobacterium sp. Strain StRB126

AidC, a Novel N -Acylhomoserine Lactonase from the Potato Root-Associated Cytophaga-Flavobacteria-Bacteroides (CFB) Group Bacterium Chryseobacterium sp. Strain StRB126

AmiE, a Novel N -Acylhomoserine Lactone Acylase Belonging to the Amidase Family, from the Activated-Sludge Isolate Acinetobacter sp. Strain Ooi24

Characterization of a novel thermostable N-acylhomoserine lactonase from the thermophilic bacterium Thermaerobacter marianensis

Contact Info

Product

Resources

About