Crystal structure of thermostable alkylsulfatase SdsAP from <i>Pseudomonas sp. S9</i>

Sun, Lifang; Chen, Pu; Y, Su; Cai, Zhixiong; Ruan, Lingwei; Xu, Xun; Wu, Yunkun

doi:10.1042/bsr20170001

Cited by 3 publications

(2 citation statements)

References 30 publications

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“…Mutations of residues Tyr246 and Gly263 of SdsAP, a type III sulfatase in Pseudomonas sp. S9, show that the mutants abolish the enzyme activity for SDS degradation, indicating that these residues are important for the functions of type III sulfatases [ 39 ].…”

Section: Introductionmentioning

confidence: 99%

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MaAts, an Alkylsulfatase, Contributes to Fungal Tolerances against UV-B Irradiation and Heat-Shock in Metarhizium acridum

Song

Xia

Wang

et al. 2022

JoF

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Sulfatases are commonly divided into three classes: type I, type II, and type III sulfatases. The type III sulfatase, alkylsulfatase, could hydrolyze the primary alkyl sulfates, such as sodium dodecyl sulfate (SDS) and sodium octyl sulfate. Thus, it has the potential application of SDS biodegradation. However, the roles of alkylsulfatase in biological control fungus remain unclear. In this study, an alkylsulfatase gene MaAts was identified from Metarhizium acridum. The deletion strain (ΔMaAts) and the complemented strain (CP) were constructed to reveal their functions in M. acridum. The activity of alkylsulfatase in ΔMaAts was dramatically reduced compared to the wild-type (WT) strain. The loss of MaAts delayed conidial germination, conidiation, and significantly declined the fungal tolerances to UV-B irradiation and heat-shock, while the fungal conidial yield and virulence were unaffected in M. acridum. The transcription levels of stress resistance-related genes were significantly changed after MaAts inactivation. Furthermore, digital gene expression profiling showed that 512 differential expression genes (DEGs), including 177 up-regulated genes and 335 down-regulated genes in ΔMaAts, were identified. Of these DEGs, some genes were involved in melanin synthesis, cell wall integrity, and tolerances to various stresses. These results indicate that MaAts and the DEGs involved in fungal stress tolerances may be candidate genes to be adopted to improve the stress tolerances of mycopesticides.

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Section: Introductionmentioning

confidence: 99%

“…To date, type III sulfatases were found and identified mainly in microorganisms, with a focus on the identification of the crystal structure [ 39 ] and the activities in degrading a surfactant [ 40 ]. In Pseudomonas sp.…”

Section: Introductionmentioning

confidence: 99%

MaAts, an Alkylsulfatase, Contributes to Fungal Tolerances against UV-B Irradiation and Heat-Shock in Metarhizium acridum

Song

Xia

Wang

et al. 2022

JoF

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Alkyl Sulfatase of Cholera Vibrios

Duvanova,

Podoinitsyna,

Pisanov

et al. 2023

Problemy Osobo Opasnykh Infektsii

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The aim of the work was to study the structure of the alkyl sulfatase (asu) gene in Vibrio cholerae strains of various serogroups, as well as to compare nucleotide and amino acid sequences of alkyl sulfatases using various methods of bioinformatic analysis.Materials and methods. 483 strains of V. cholerae O1, O139 and nonO1/nonO139 serogroups were employed in the work. The search for the gene, its recurrence, and localization was carried out applying the Blast software. The nucleotide and corresponding amino acid sequences of the gene, as well as its structure, were studied using bioinformatic analysis. Sequencing was performed on the MiSeq (Illumina) platform. The enzymatic activity was detected using a medium, confirming the presence/absence of the gene by PCR in vitro and in silico.Results and discussion. Bioinformatic analysis of the nucleotide and corresponding amino acid sequences of the asu gene has been carried out and its structure investigated. Four functional domains have been identified. In the beta-lactamase domain, a conservative amino acid sequence -HAHADH- has been found in all strains of cholera vibrios, which is part of the Zn2+ binding motif. It has been established that the alkyl sulfatase of cholera vibrios belongs to the family of Zn2+-dependent β-lactamases. Blast analysis has revealed the similarity of nucleotide and amino acid sequences of alkyl sulfatases in representatives of V. cholerae O1 and O139 serogroups (ctxAB+tcpA+) and representatives of the genera Aeromonas and Pseudomonas, which is in the line with the data of 3D modeling of the amino acid sequence structures of the alkyl sulfatase enzyme in these microorganisms. The bioinformatic analysis of nucleotide and amino acid sequences of alkyl sulfatases in cholera vibrios has showed the conservativeness of these sequences in toxigenic strains and the presence of a number of single mutations in the asu gene in atoxigenic ones. The presence or absence of the asu gene has been established by PCR in vitro and in silico and confirmed by the results obtained using the Blast program. It is demonstrated that the presence/absence of the asu gene correlates with the ability/inability of O139 strains to hydrolyze SDS on the medium. These results can be used in studying mechanisms of cholera vibrios adaptation, persistence and pathogenicity.

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Characterization and Structural Insights of a Novel Arylsulfatase from Pseudoalteromonas atlantica T6c

et al. 2023

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Arylsulfatases exhibit great potential in industry for desulfation applications, but less is known about the metallo-β-lactamase (MBL) fold arylsulfatases. To learn more about them, an MBL fold arylsulfatase from Pseudoalteromonas atlantica T6c (PaAst) was identified and characterized, and its structure was elaborated in this study. PaAst was sequence analyzed, heterologously expressed in E. coli, purified by Ni2+-NTA resin affinity chromatography and size-exclusion chromatography, functionally studied by p-nitrophenyl sulfate (pNPS), and crystallized for structure determination. The MBL fold arylsulfatase was identified by sequence analysis and confirmed by enzymatic assay on pNPS with Km 1.00 mM and Vmax 60.80 U/mg at 50 °C and pH 7.5. Furthermore, its crystals were obtained in 0.2 M sodium thiocyamate, 20% PEG3350, and its structure was determined at 2.0 Å that formed a dimer with MBL fold. Our work highlighted the MBL fold arylsulfatases from structural insights and could be the theoretical foundation for investigations into their catalytic mechanism.

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Crystal structure of thermostable alkylsulfatase SdsAP from Pseudomonas sp. S9

Cited by 3 publications

References 30 publications

MaAts, an Alkylsulfatase, Contributes to Fungal Tolerances against UV-B Irradiation and Heat-Shock in Metarhizium acridum

MaAts, an Alkylsulfatase, Contributes to Fungal Tolerances against UV-B Irradiation and Heat-Shock in Metarhizium acridum

Alkyl Sulfatase of Cholera Vibrios

Characterization and Structural Insights of a Novel Arylsulfatase from Pseudoalteromonas atlantica T6c

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