Structural and enzymatic characterization of the lactonase SisLac from Sulfolobus islandicus.

<h4>Background</h4>A new member of the Phosphotriesterase-Like Lactonases (PLL) family from the hyperthermophilic archeon Sulfolobus islandicus (SisLac) has been characterized. SisLac is a native lactonase that exhibits a high promiscuous phosphotriesterase activity. SisLac thus represen...

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Autores principales:	Julien Hiblot, Guillaume Gotthard, Eric Chabriere, Mikael Elias
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/fc0c768cf95844939e568bafdc56ce90
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spelling	oai:doaj.org-article:fc0c768cf95844939e568bafdc56ce902021-11-18T08:12:31ZStructural and enzymatic characterization of the lactonase SisLac from Sulfolobus islandicus.1932-620310.1371/journal.pone.0047028https://doaj.org/article/fc0c768cf95844939e568bafdc56ce902012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23071703/?tool=EBIhttps://doaj.org/toc/1932-6203<h4>Background</h4>A new member of the Phosphotriesterase-Like Lactonases (PLL) family from the hyperthermophilic archeon Sulfolobus islandicus (SisLac) has been characterized. SisLac is a native lactonase that exhibits a high promiscuous phosphotriesterase activity. SisLac thus represents a promising target for engineering studies, exhibiting both detoxification and bacterial quorum quenching abilities, including human pathogens such as Pseudomonas aeruginosa.<h4>Methodology/principal findings</h4>Here, we describe the substrate specificity of SisLac, providing extensive kinetic studies performed with various phosphotriesters, esters, N-acyl-homoserine lactones (AHLs) and other lactones as substrates. Moreover, we solved the X-ray structure of SisLac and structural comparisons with the closely related SsoPox structure highlighted differences in the surface salt bridge network and the dimerization interface. SisLac and SsoPox being close homologues (91% sequence identity), we undertook a mutational study to decipher these structural differences and their putative consequences on the stability and the catalytic properties of these proteins.<h4>Conclusions/significance</h4>We show that SisLac is a very proficient lactonase against aroma lactones and AHLs as substrates. Hence, data herein emphasize the potential role of SisLac as quorum quenching agent in Sulfolobus. Moreover, despite the very high sequence homology with SsoPox, we highlight key epistatic substitutions that influence the enzyme stability and activity.Julien HiblotGuillaume GotthardEric ChabriereMikael EliasPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 10, p e47028 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Julien Hiblot Guillaume Gotthard Eric Chabriere Mikael Elias Structural and enzymatic characterization of the lactonase SisLac from Sulfolobus islandicus.
description	<h4>Background</h4>A new member of the Phosphotriesterase-Like Lactonases (PLL) family from the hyperthermophilic archeon Sulfolobus islandicus (SisLac) has been characterized. SisLac is a native lactonase that exhibits a high promiscuous phosphotriesterase activity. SisLac thus represents a promising target for engineering studies, exhibiting both detoxification and bacterial quorum quenching abilities, including human pathogens such as Pseudomonas aeruginosa.<h4>Methodology/principal findings</h4>Here, we describe the substrate specificity of SisLac, providing extensive kinetic studies performed with various phosphotriesters, esters, N-acyl-homoserine lactones (AHLs) and other lactones as substrates. Moreover, we solved the X-ray structure of SisLac and structural comparisons with the closely related SsoPox structure highlighted differences in the surface salt bridge network and the dimerization interface. SisLac and SsoPox being close homologues (91% sequence identity), we undertook a mutational study to decipher these structural differences and their putative consequences on the stability and the catalytic properties of these proteins.<h4>Conclusions/significance</h4>We show that SisLac is a very proficient lactonase against aroma lactones and AHLs as substrates. Hence, data herein emphasize the potential role of SisLac as quorum quenching agent in Sulfolobus. Moreover, despite the very high sequence homology with SsoPox, we highlight key epistatic substitutions that influence the enzyme stability and activity.
format	article
author	Julien Hiblot Guillaume Gotthard Eric Chabriere Mikael Elias
author_facet	Julien Hiblot Guillaume Gotthard Eric Chabriere Mikael Elias
author_sort	Julien Hiblot
title	Structural and enzymatic characterization of the lactonase SisLac from Sulfolobus islandicus.
title_short	Structural and enzymatic characterization of the lactonase SisLac from Sulfolobus islandicus.
title_full	Structural and enzymatic characterization of the lactonase SisLac from Sulfolobus islandicus.
title_fullStr	Structural and enzymatic characterization of the lactonase SisLac from Sulfolobus islandicus.
title_full_unstemmed	Structural and enzymatic characterization of the lactonase SisLac from Sulfolobus islandicus.
title_sort	structural and enzymatic characterization of the lactonase sislac from sulfolobus islandicus.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/fc0c768cf95844939e568bafdc56ce90
work_keys_str_mv	AT julienhiblot structuralandenzymaticcharacterizationofthelactonasesislacfromsulfolobusislandicus AT guillaumegotthard structuralandenzymaticcharacterizationofthelactonasesislacfromsulfolobusislandicus AT ericchabriere structuralandenzymaticcharacterizationofthelactonasesislacfromsulfolobusislandicus AT mikaelelias structuralandenzymaticcharacterizationofthelactonasesislacfromsulfolobusislandicus
_version_	1718422084462313472

Structural and enzymatic characterization of the lactonase SisLac from Sulfolobus islandicus.

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