Structural and physiological analyses of the alkanesulphonate-binding protein (SsuA) of the citrus pathogen Xanthomonas citri.
Identifieur interne : 000411 ( PubMed/Corpus ); précédent : 000410; suivant : 000412Structural and physiological analyses of the alkanesulphonate-binding protein (SsuA) of the citrus pathogen Xanthomonas citri.
Auteurs : Fabiano T Foli De Araújo ; Victor M. Bolanos-Garcia ; Cristiane T. Pereira ; Mario Sanches ; Elisa E. Oshiro ; Rita C C. Ferreira ; Dimitri Y. Chigardze ; João Alexandre Gonçalves Barbosa ; Luís Carlos De Souza Ferreira ; Celso E. Benedetti ; Tom L. Blundell ; Andrea BalanSource :
- PloS one [ 1932-6203 ] ; 2013.
English descriptors
- KwdEn :
- Alkanesulfonates (chemistry), Alkanesulfonates (metabolism), Amino Acid Sequence, Bacterial Proteins (chemistry), Bacterial Proteins (genetics), Bacterial Proteins (physiology), Binding Sites, Carrier Proteins (chemistry), Carrier Proteins (genetics), Carrier Proteins (physiology), Citrus sinensis (growth & development), Citrus sinensis (metabolism), Citrus sinensis (microbiology), Models, Molecular, Molecular Sequence Data, Plant Diseases (microbiology), Polysaccharides, Bacterial (metabolism), Sequence Alignment, Virulence, X-Ray Diffraction, Xanthomonas (genetics), Xanthomonas (metabolism), Xanthomonas (pathogenicity).
- MESH :
- chemical , chemistry : Alkanesulfonates, Bacterial Proteins, Carrier Proteins.
- chemical , genetics : Bacterial Proteins, Carrier Proteins.
- chemical , metabolism : Alkanesulfonates, Polysaccharides, Bacterial.
- chemical , physiology : Bacterial Proteins, Carrier Proteins.
- genetics : Xanthomonas.
- growth & development : Citrus sinensis.
- metabolism : Citrus sinensis, Xanthomonas.
- microbiology : Citrus sinensis, Plant Diseases.
- pathogenicity : Xanthomonas.
- Amino Acid Sequence, Binding Sites, Models, Molecular, Molecular Sequence Data, Sequence Alignment, Virulence, X-Ray Diffraction.
Abstract
The uptake of sulphur-containing compounds plays a pivotal role in the physiology of bacteria that live in aerobic soils where organosulfur compounds such as sulphonates and sulphate esters represent more than 95% of the available sulphur. Until now, no information has been available on the uptake of sulphonates by bacterial plant pathogens, particularly those of the Xanthomonas genus, which encompasses several pathogenic species. In the present study, we characterised the alkanesulphonate uptake system (Ssu) of Xanthomonas axonopodis pv. citri 306 strain (X. citri), the etiological agent of citrus canker.
DOI: 10.1371/journal.pone.0080083
PubMed: 24282519
Links to Exploration step
pubmed:24282519Le document en format XML
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<term>Bacterial Proteins (chemistry)</term>
<term>Bacterial Proteins (genetics)</term>
<term>Bacterial Proteins (physiology)</term>
<term>Binding Sites</term>
<term>Carrier Proteins (chemistry)</term>
<term>Carrier Proteins (genetics)</term>
<term>Carrier Proteins (physiology)</term>
<term>Citrus sinensis (growth & development)</term>
<term>Citrus sinensis (metabolism)</term>
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<term>Molecular Sequence Data</term>
<term>Plant Diseases (microbiology)</term>
<term>Polysaccharides, Bacterial (metabolism)</term>
<term>Sequence Alignment</term>
<term>Virulence</term>
<term>X-Ray Diffraction</term>
<term>Xanthomonas (genetics)</term>
<term>Xanthomonas (metabolism)</term>
<term>Xanthomonas (pathogenicity)</term>
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<term>Carrier Proteins</term>
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<term>Carrier Proteins</term>
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<term>Polysaccharides, Bacterial</term>
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<term>Carrier Proteins</term>
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<term>Binding Sites</term>
<term>Models, Molecular</term>
<term>Molecular Sequence Data</term>
<term>Sequence Alignment</term>
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<front><div type="abstract" xml:lang="en">The uptake of sulphur-containing compounds plays a pivotal role in the physiology of bacteria that live in aerobic soils where organosulfur compounds such as sulphonates and sulphate esters represent more than 95% of the available sulphur. Until now, no information has been available on the uptake of sulphonates by bacterial plant pathogens, particularly those of the Xanthomonas genus, which encompasses several pathogenic species. In the present study, we characterised the alkanesulphonate uptake system (Ssu) of Xanthomonas axonopodis pv. citri 306 strain (X. citri), the etiological agent of citrus canker.</div>
</front>
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<Issue>11</Issue>
<PubDate><Year>2013</Year>
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<Title>PloS one</Title>
<ISOAbbreviation>PLoS ONE</ISOAbbreviation>
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<ArticleTitle>Structural and physiological analyses of the alkanesulphonate-binding protein (SsuA) of the citrus pathogen Xanthomonas citri.</ArticleTitle>
<Pagination><MedlinePgn>e80083</MedlinePgn>
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<Abstract><AbstractText Label="BACKGROUND" NlmCategory="BACKGROUND">The uptake of sulphur-containing compounds plays a pivotal role in the physiology of bacteria that live in aerobic soils where organosulfur compounds such as sulphonates and sulphate esters represent more than 95% of the available sulphur. Until now, no information has been available on the uptake of sulphonates by bacterial plant pathogens, particularly those of the Xanthomonas genus, which encompasses several pathogenic species. In the present study, we characterised the alkanesulphonate uptake system (Ssu) of Xanthomonas axonopodis pv. citri 306 strain (X. citri), the etiological agent of citrus canker.</AbstractText>
<AbstractText Label="METHODOLOGY/PRINCIPAL FINDINGS" NlmCategory="RESULTS">A single operon-like gene cluster (ssuEDACB) that encodes both the sulphur uptake system and enzymes involved in desulphurisation was detected in the genomes of X. citri and of the closely related species. We characterised X. citri SsuA protein, a periplasmic alkanesulphonate-binding protein that, together with SsuC and SsuB, defines the alkanesulphonate uptake system. The crystal structure of SsuA bound to MOPS, MES and HEPES, which is herein described for the first time, provides evidence for the importance of a conserved dipole in sulphate group coordination, identifies specific amino acids interacting with the sulphate group and shows the presence of a rather large binding pocket that explains the rather wide range of molecules recognised by the protein. Isolation of an isogenic ssuA-knockout derivative of the X. citri 306 strain showed that disruption of alkanesulphonate uptake affects both xanthan gum production and generation of canker lesions in sweet orange leaves.</AbstractText>
<AbstractText Label="CONCLUSIONS/SIGNIFICANCE" NlmCategory="CONCLUSIONS">The present study unravels unique structural and functional features of the X. citri SsuA protein and provides the first experimental evidence that an ABC uptake system affects the virulence of this phytopathogen.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Tófoli de Araújo</LastName>
<ForeName>Fabiano</ForeName>
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<AffiliationInfo><Affiliation>Departamento de Microbiologia, Universidade de São Paulo, São Paulo, São Paulo, Brazil.</Affiliation>
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<Author ValidYN="Y"><LastName>Bolanos-Garcia</LastName>
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<Author ValidYN="Y"><LastName>Pereira</LastName>
<ForeName>Cristiane T</ForeName>
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<ForeName>João Alexandre Gonçalves</ForeName>
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<Author ValidYN="Y"><LastName>de Souza Ferreira</LastName>
<ForeName>Luís Carlos</ForeName>
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<Author ValidYN="Y"><LastName>Benedetti</LastName>
<ForeName>Celso E</ForeName>
<Initials>CE</Initials>
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<Author ValidYN="Y"><LastName>Blundell</LastName>
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