Arylsulphatase from Alteromonas carrageenovora

Barbeyron, Tristan; Potin, Philippe; Richard, Christophe; Collin, Olivier; Kloareg, Bernard

doi:10.1099/13500872-141-11-2897

Cited by 52 publications

(38 citation statements)

References 35 publications

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“…The few exceptions may have resulted from different cultivation conditions or different phenotypic tests. The major discrepancies with the original description of the genus Maribacter and the five Maribacter species in this study are: (i) agarase activity was not detected in any strain; (ii) DNA hydrolysis was detected in all species except M. aquivivus; and (iii) although tested several times (five experiments), none of the species was able to reduce nitrate to nitrite in API 20 NE strips (a result confirmed using the Greiss reagent and strain Zobellia galactanivorans Dsij T as positive control; Barbeyron et al, 2001). Moreover, in contrast with the statements of Nedashkovskaya et al (2004) and Yoon et al (2005), strains KT02ds18-4, KT02ds18-5 and KT02ds18-6 T were able to grow, albeit weakly, in the absence of NaCl.…”

supporting

confidence: 57%

Description of Maribacter forsetii sp. nov., a marine Flavobacteriaceae isolated from North Sea water, and emended description of the genus Maribacter

Barbeyron

Carpentier

L’Haridon

et al. 2008

INTERNATIONAL JOURNAL OF SYSTEMATIC AND EVOLUTIONARY MICROBIOLO

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This is an author manuscript that has been accepted for publication in International Journal of Systematic and Evolutionary Microbiology, copyright Society for General Microbiology, but has not been copy-edited, formatted or proofed. Cite this article as appearing in International Journal of Systematic and Evolutionary Microbiology. This version of the manuscript may not be duplicated or reproduced, other than for personal use or within the rule of 'Fair Use of Copyrighted Materials' (section 17, Title 17, US Code), without permission from the copyright owner, Society for General Microbiology. The Society for General Microbiology disclaims any responsibility or liability for errors or omissions in this version of the manuscript or in any version derived from it by any other parties. The final copy-edited, published article, which is the version of record, can be found at http://mic.sgmjournals.org, and is freely available without a subscription.International audienceThree rod-shaped, Gram-negative, chemo-organotrophic, heterotrophic, strictly aerobic, gliding bacterial strains, KT02ds18-4, KT02ds18-5 and KT02ds18-6T, were isolated from North Sea surface waters near the island of Helgoland, Germany. Their taxonomic position was investigated by a polyphasic approach. The three strains were light yellow, oxidase- and catalase-positive, and grew optimally at 25 degrees C, at pH 7.5, and in the presence of 2.5 % (w/v) NaCl. The Chargaff's coefficient was 34.2-34.4 mol%. The three strains shared >90 % DNA-DNA relatedness and an identical 16S rRNA gene sequence. Comparative 16S rRNA gene sequence analysis allocated the three strains to the genus Maribacter in the family Flavobacteriaceae, with similarities of 97.0-97.4 % to five of the recognized Maribacter species. Their low level of DNA-DNA relatedness (<20 %) with these species and differentiating phenotypic characteristics demonstrated that they constitute a new Maribacter species for which the name Maribacter forsetii sp. nov. is proposed. Strain KT02ds18-6T (=CIP 109504T=DSM 18668T) is the type strain. An emended description of the genus Maribacter is also proposed

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supporting

confidence: 57%

Description of Maribacter forsetii sp. nov., a marine Flavobacteriaceae isolated from North Sea water, and emended description of the genus Maribacter

Barbeyron

Carpentier

L’Haridon

et al. 2008

INTERNATIONAL JOURNAL OF SYSTEMATIC AND EVOLUTIONARY MICROBIOLO

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“…These enzymes oxidatively cleave sulfate esters into inorganic sulfate and the corresponding aldehyde and require ␣-ketoglutarate as a cosubstrate (6). Evidence for a third group of sulfatases (group III) has accumulated over many years (7)(8)(9)(10)(11). However, the fact that Pseudomonas aeruginosa strains express up to six alkyl-or arylsulfatases (12), compounded by a lack of sequence data for the zymographically identified enzymes, confused the issue and prevented their identification as a distinct group.…”

mentioning

confidence: 99%

The crystal structure of SdsA1, an alkylsulfatase from Pseudomonas aeruginosa , defines a third class of sulfatases

Hagelueken

Adams

Wiehlmann

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

118

148

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authors note that Fig. 5 did not include all vaccine study groups. The corrected figure and legend appear below. This error does not affect the conclusions of the article. Confidence intervals for Spearman's rank correlation of log 10 IFN-␥ producing PBMC per million and log10 stimulation index were based on Fisher's transformation. On day 14, the correlation was 0.491 (95% CI, 0.231-0.686); on day 28, the correlation was 0.188 (95% CI: Ϫ0.112 to 0.456).

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“…The domain forms the catalytic center of three unrelated enzymes: metallo-␤-lactamase, glyoxylase II, and a less-well-characterized bacterial arylsulfatase, which hydrolyze amide, thiolester, and sulfate ester bonds, respectively (Barbeyron et al, 1995;Carfi et al, 1995;Cameron et al, 1999). A histidine-rich metal-binding domain is also essential for catalysis in the cNMP phosphodiesterases, but the configuration of the histidines in this domain is entirely different (Xu et al, 2000).…”

Section: Discussionmentioning

confidence: 99%

Identification of a Novel Type of cGMP Phosphodiesterase That Is Defective in the ChemotacticstmFMutants

Meima

Biondi

Schaap

2002

MBoC

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StmF mutants are chemotactic mutants that are defective in a cGMP phosphodiesterase (PDE) activity. We identified a novel gene, PdeD, that harbors two cyclic nucleotide-binding domains and a metallo-␤-lactamase homology domain. Similar to stmF mutants, pdeD-null mutants displayed extensively streaming aggregates, prolonged elevation of cGMP levels after chemotactic stimulation, and reduced cGMP-PDE activity. PdeD transcripts were lacking in stmF mutant NP377, indicating that this mutant carries a PdeD lesion. Expression of a PdeD-YFP fusion protein in pdeD-null cells restored the normal cGMP response and showed that PdeD resides in the cytosol. When purified by immunoprecipitation, the PdeD-YFP fusion protein displayed cGMP-PDE activity, which was retained in a truncated construct that contained only the metallo-␤-lactamase domain. Newell, 1979, 1981;Kuwayama et al., 1993). Mutants KI8 and KI10 show no ligand-induced cGMP response and cannot chemotax (Kuwayama et al., 1993). Streamer F (stmF) mutants are defective in cGMP-PDE activity (Van Haastert et al., 1982). These mutants show an elevated and prolonged cGMP response and prolonged association of myosin with the cytoskeleton (Ross and Newell, 1981;Liu and Newell, 1988, 1994. When grown as colonies on dense bacterial lawns, stmF mutants form aggregates with very pronounced aggregation streams, a phenotype that under these conditions is not displayed by wild-type cells. INTRODUCTION Mutants in cGMP metabolism have implicated cGMP as intermediate for ligand-induced chemotaxis in DictyosteliumThree PDE genes have been identified in Dictyostelium; two of those, RegA (Shaulsky et al., 1996;Thomason et al., 1998) and PDE3 (Kuwayama et al., 2001), belong to the large class of HD-domain PDEs that is commonly found in vertebrates (Mehats et al., 2002). The third enzyme, PdsA (Lacombe et al., 1986), is a class II PDE that is also found in yeast (Nikawa et al., 1987). None of these genes are associated with the stmF locus.In our search for targets of cyclic nucleotides, we identified a gene, PdeD, with two putative cyclic nucleotide (cNMP)-binding domains and a binuclear Zn 2ϩ -binding domain. The latter domain forms the catalytic center of bacterial metallo-␤-lactamases, which hydrolyze an amide bond in the ␤-lactam ring of carbapenem antibiotics (Carfi et al., 1995) and are a major cause for widespread bacterial antibiotic resistance (Payne, 1993). We show that pdeD-null mutants phenocopy stmF mutants. One of the cNMP-binding domains of PdeD most likely functions as an allosteric activator of the enzyme, whereas the metallo-␤-lactamase homology domain catalyzes the hydrolysis of cGMP. MATERIALS AND METHODS Cell Growth and DevelopmentD. discoideum strains NC4, XP55, and NP377 were grown in association with Klebsiella aerogenes on SM agar plates, and all other strains were grown in HL5 medium, supplemented with 5 g/ml blasticidin or 20 -200 g/ml G418 for strains transformed with pBsr⌬Bam or neomycin selection markers, respectively. For developmental time courses, cells ...

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Arylsulphatase from Alteromonas carrageenovora

Cited by 52 publications

References 35 publications

Description of Maribacter forsetii sp. nov., a marine Flavobacteriaceae isolated from North Sea water, and emended description of the genus Maribacter

Description of Maribacter forsetii sp. nov., a marine Flavobacteriaceae isolated from North Sea water, and emended description of the genus Maribacter

The crystal structure of SdsA1, an alkylsulfatase from Pseudomonas aeruginosa , defines a third class of sulfatases

Identification of a Novel Type of cGMP Phosphodiesterase That Is Defective in the ChemotacticstmFMutants

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