Soil metagenome-derived 3-hydroxypalmitic acid methyl ester hydrolases suppress extracellular polysaccharide production in Ralstonia solanacearum

Published on Mar 1, 2018in Journal of Biomedical Informatics2.95
· DOI :10.1016/j.jbiotec.2018.01.023
Myung Hwan Lee9
Estimated H-index: 9
(Dong-a University),
Raees Khan4
Estimated H-index: 4
(Dong-a University)
+ 5 AuthorsSeon-Woo Lee12
Estimated H-index: 12
(Dong-a University)
Abstract Autoinducers are indispensable for bacterial cell–cell communication. However, due to the reliance on culture-based techniques, few autoinducer-hydrolyzing enzymes are known. In this study, we characterized soil metagenome-derived unique enzymes capable of hydrolyzing 3-hydroxypalmitic acid methyl ester (3-OH PAME), an autoinducer of the plant pathogenic bacterium Ralstonia solanacearum. Among 146 candidate lipolytic clones from a soil metagenome library, 4 unique enzymes capable of hydrolyzing the autoinducer 3-OH PAME, termed ELP86, ELP96, ELP104, and EstDL33, were selected and characterized. Phylogenetic analysis revealed that metagenomic enzymes were novel esterase/lipase candidates as they clustered as novel subfamilies of family I, V, X, and family XI. The purified enzymes displayed various levels of hydrolytic activities towards 3-OH PAME with optimum activity at 40–50 °C and pH 7–10. Interestingly, ELP104 also displayed N-(3-oxohexanoyl)-L-homoserine lactone hydrolysis activity. Heterologous expression of the gene encoding 3-OH PAME hydrolase in R. solanacearum significantly decreased exopolysaccharide production without affecting bacterial growth. mRNA transcription analysis revealed that genes regulated by quorum-sensing, such as phcA and xpsR, were significantly down-regulated in the stationary growth phase of R. solanacearum. Therefore, metagenomic enzymes are capable of quorum-quenching by hydrolyzing the autoinducer 3-OH PAME, which could be used as a biocontrol strategy against bacterial wilt.
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#1Sudhir Kumar (TU: Temple University)H-Index: 65
#2Glen Stecher (TU: Temple University)H-Index: 7
Last.Koichiro Tamura (Tokyo Metropolitan University)H-Index: 29
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#1Kenji Kai (OPU: Osaka Prefecture University)H-Index: 13
#2Hideyuki Ohnishi (OPU: Osaka Prefecture University)H-Index: 4
Last.Yasufumi Hikichi (Kōchi University)H-Index: 23
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#1Nicolas Lenfant (CNRS: Centre national de la recherche scientifique)H-Index: 12
#2Thierry Hotelier (CNRS: Centre national de la recherche scientifique)H-Index: 9
Last.Arnaud Chatonnet (CNRS: Centre national de la recherche scientifique)H-Index: 27
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#1Weixin Tao (Dong-a University)H-Index: 10
#2Myung Hwan Lee (Dong-a University)H-Index: 9
Last.Seon-Woo Lee (Dong-a University)H-Index: 12
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#1Patrick Bijtenhoorn (UHH: University of Hamburg)H-Index: 1
#2Hubert Mayerhofer (EMBL-EBI: European Bioinformatics Institute)H-Index: 8
Last.Wolfgang R. Streit (UHH: University of Hamburg)H-Index: 37
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