Glutaredoxin-like protein (GLP)-a novel bacteria sulfurtransferase that protects cells against cyanide and oxidative stresses.
Identifieur interne : 000065 ( Main/Exploration ); précédent : 000064; suivant : 000066Glutaredoxin-like protein (GLP)-a novel bacteria sulfurtransferase that protects cells against cyanide and oxidative stresses.
Auteurs : Carla Peres De Paula [Brésil] ; Melina Cardoso Dos Santos [Brésil] ; Carlos A. Tairum [Brésil] ; Carlos Alexandre Breyer [Brésil] ; Guilherme Toledo-Silva [Brésil] ; Marcos Hikari Toyama [Brésil] ; Gustavo Maruyama Mori [Brésil] ; Marcos Antonio De Oliveira [Brésil]Source :
- Applied microbiology and biotechnology [ 1432-0614 ] ; 2020.
Abstract
The pathogen Xylella fastidiosa belongs to the Xanthomonadaceae family, a large group of Gram-negative bacteria that cause diseases in many economically important crops. A predicted gene, annotated as glutaredoxin-like protein (glp), was found to be highly conserved among the genomes of different genera within this family and highly expressed in X. fastidiosa. Analysis of the GLP protein sequences revealed three protein domains: one similar to monothiol glutaredoxins (Grx), an Fe-S cluster and a thiosulfate sulfurtransferase/rhodanese domain (Tst/Rho), which is generally involved in sulfur metabolism and cyanide detoxification. To characterize the biochemical properties of GLP, we expressed and purified the X. fastidiosa recombinant GLP enzyme. Grx activity and Fe-S cluster formation were not observed, while an evaluation of Tst/Rho enzymatic activity revealed that GLP can detoxify cyanide and transfer inorganic sulfur to acceptor molecules in vitro. The biological activity of GLP relies on the cysteine residues in the Grx and Tst/Rho domains (Cys33 and Cys266, respectively), and structural analysis showed that GLP and GLPC266S were able to form high molecular weight oligomers (> 600 kDa), while replacement of Cys33 with Ser destabilized the quaternary structure. In vivo heterologous enzyme expression experiments in Escherichia coli revealed that GLP can protect bacteria against high concentrations of cyanide and hydrogen peroxide. Finally, phylogenetic analysis showed that homologous glp genes are distributed across Gram-negative bacterial families with conservation of the N- to C-domain order. However, no eukaryotic organism contains this enzyme. Altogether, these results suggest that GLP is an important enzyme with cyanide-decomposing and sulfurtransferase functions in bacteria, whose presence in eukaryotes we could not observe, representing a promising biological target for new pharmaceuticals.
DOI: 10.1007/s00253-020-10491-5
PubMed: 32307572
Affiliations:
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São Paulo State University, São Vicente, SP, Brazil. mao@clp.unesp.br.</nlm:affiliation><country xml:lang="fr">Brésil</country><wicri:regionArea>Laboratory of Structural Molecular Biology, Biosciences Institute, UNESP - São Paulo State University, São Vicente, SP</wicri:regionArea><placeName><region type="state">État de São Paulo</region></placeName></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2020">2020</date><idno type="RBID">pubmed:32307572</idno><idno type="pmid">32307572</idno><idno type="doi">10.1007/s00253-020-10491-5</idno><idno type="wicri:Area/Main/Corpus">000063</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000063</idno><idno type="wicri:Area/Main/Curation">000063</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000063</idno><idno type="wicri:Area/Main/Exploration">000063</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Glutaredoxin-like protein (GLP)-a novel bacteria sulfurtransferase that protects cells against cyanide and oxidative stresses.</title><author><name sortKey="De Paula, Carla Peres" sort="De Paula, Carla Peres" uniqKey="De Paula C" first="Carla Peres" last="De Paula">Carla Peres De Paula</name><affiliation wicri:level="2"><nlm:affiliation>Laboratory of Structural Molecular Biology, Biosciences Institute, UNESP - São Paulo State University, São Vicente, SP, Brazil.</nlm:affiliation><country xml:lang="fr">Brésil</country><wicri:regionArea>Laboratory of Structural Molecular Biology, Biosciences Institute, UNESP - São Paulo State University, São Vicente, SP</wicri:regionArea><placeName><region type="state">État de São Paulo</region></placeName></affiliation></author><author><name sortKey="Dos Santos, Melina Cardoso" sort="Dos Santos, Melina Cardoso" uniqKey="Dos Santos M" first="Melina Cardoso" last="Dos Santos">Melina Cardoso Dos Santos</name><affiliation wicri:level="2"><nlm:affiliation>Laboratory of Structural Molecular Biology, Biosciences Institute, UNESP - São Paulo State University, São Vicente, SP, Brazil.</nlm:affiliation><country xml:lang="fr">Brésil</country><wicri:regionArea>Laboratory of Structural Molecular Biology, Biosciences Institute, UNESP - São Paulo State University, São Vicente, SP</wicri:regionArea><placeName><region type="state">État de São Paulo</region></placeName></affiliation></author><author><name sortKey="Tairum, Carlos A" sort="Tairum, Carlos A" uniqKey="Tairum C" first="Carlos A" last="Tairum">Carlos A. Tairum</name><affiliation wicri:level="2"><nlm:affiliation>Laboratory of Structural Molecular Biology, Biosciences Institute, UNESP - São Paulo State University, São Vicente, SP, Brazil.</nlm:affiliation><country xml:lang="fr">Brésil</country><wicri:regionArea>Laboratory of Structural Molecular Biology, Biosciences Institute, UNESP - São Paulo State University, São Vicente, SP</wicri:regionArea><placeName><region type="state">État de São Paulo</region></placeName></affiliation></author><author><name sortKey="Breyer, Carlos Alexandre" sort="Breyer, Carlos Alexandre" uniqKey="Breyer C" first="Carlos Alexandre" last="Breyer">Carlos Alexandre Breyer</name><affiliation wicri:level="2"><nlm:affiliation>Laboratory of Structural Molecular Biology, Biosciences Institute, UNESP - São Paulo State University, São Vicente, SP, Brazil.</nlm:affiliation><country xml:lang="fr">Brésil</country><wicri:regionArea>Laboratory of Structural Molecular Biology, Biosciences Institute, UNESP - São Paulo State University, São Vicente, SP</wicri:regionArea><placeName><region type="state">État de São Paulo</region></placeName></affiliation></author><author><name sortKey="Toledo Silva, Guilherme" sort="Toledo Silva, Guilherme" uniqKey="Toledo Silva G" first="Guilherme" last="Toledo-Silva">Guilherme Toledo-Silva</name><affiliation wicri:level="2"><nlm:affiliation>Laboratory of Biomarkers of Aquatic Contamination and Immunochemistry, Department of Biochemistry, Federal University of Santa Catarina, Florianopolis, SC, Brazil.</nlm:affiliation><country xml:lang="fr">Brésil</country><wicri:regionArea>Laboratory of Biomarkers of Aquatic Contamination and Immunochemistry, Department of Biochemistry, Federal University of Santa Catarina, Florianopolis, SC</wicri:regionArea><placeName><region type="state">Santa Catarina</region></placeName></affiliation></author><author><name sortKey="Toyama, Marcos Hikari" sort="Toyama, Marcos Hikari" uniqKey="Toyama M" first="Marcos Hikari" last="Toyama">Marcos Hikari Toyama</name><affiliation wicri:level="2"><nlm:affiliation>Laboratory of Functional and Structural Characterization of Toxins of Venomous and Poisonous Animals, Biosciences Institute, UNESP - São Paulo State University, São Vicente, SP, Brazil.</nlm:affiliation><country xml:lang="fr">Brésil</country><wicri:regionArea>Laboratory of Functional and Structural Characterization of Toxins of Venomous and Poisonous Animals, Biosciences Institute, UNESP - São Paulo State University, São Vicente, SP</wicri:regionArea><placeName><region type="state">État de São Paulo</region></placeName></affiliation></author><author><name sortKey="Mori, Gustavo Maruyama" sort="Mori, Gustavo Maruyama" uniqKey="Mori G" first="Gustavo Maruyama" last="Mori">Gustavo Maruyama Mori</name><affiliation wicri:level="2"><nlm:affiliation>Molecular Ecology Laboratory, Biosciences Institute, UNESP - São Paulo State University, São Vicente, SP, Brazil.</nlm:affiliation><country xml:lang="fr">Brésil</country><wicri:regionArea>Molecular Ecology Laboratory, Biosciences Institute, UNESP - São Paulo State University, São Vicente, SP</wicri:regionArea><placeName><region type="state">État de São Paulo</region></placeName></affiliation></author><author><name sortKey="De Oliveira, Marcos Antonio" sort="De Oliveira, Marcos Antonio" uniqKey="De Oliveira M" first="Marcos Antonio" last="De Oliveira">Marcos Antonio De Oliveira</name><affiliation wicri:level="2"><nlm:affiliation>Laboratory of Structural Molecular Biology, Biosciences Institute, UNESP - São Paulo State University, São Vicente, SP, Brazil. mao@clp.unesp.br.</nlm:affiliation><country xml:lang="fr">Brésil</country><wicri:regionArea>Laboratory of Structural Molecular Biology, Biosciences Institute, UNESP - São Paulo State University, São Vicente, SP</wicri:regionArea><placeName><region type="state">État de São Paulo</region></placeName></affiliation></author></analytic><series><title level="j">Applied microbiology and biotechnology</title><idno type="eISSN">1432-0614</idno><imprint><date when="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The pathogen Xylella fastidiosa belongs to the Xanthomonadaceae family, a large group of Gram-negative bacteria that cause diseases in many economically important crops. A predicted gene, annotated as glutaredoxin-like protein (glp), was found to be highly conserved among the genomes of different genera within this family and highly expressed in X. fastidiosa. Analysis of the GLP protein sequences revealed three protein domains: one similar to monothiol glutaredoxins (Grx), an Fe-S cluster and a thiosulfate sulfurtransferase/rhodanese domain (Tst/Rho), which is generally involved in sulfur metabolism and cyanide detoxification. To characterize the biochemical properties of GLP, we expressed and purified the X. fastidiosa recombinant GLP enzyme. Grx activity and Fe-S cluster formation were not observed, while an evaluation of Tst/Rho enzymatic activity revealed that GLP can detoxify cyanide and transfer inorganic sulfur to acceptor molecules in vitro. The biological activity of GLP relies on the cysteine residues in the Grx and Tst/Rho domains (Cys<sup>33</sup> and Cys<sup>266</sup>, respectively), and structural analysis showed that GLP and GLP<sup>C266S</sup> were able to form high molecular weight oligomers (> 600 kDa), while replacement of Cys<sup>33</sup> with Ser destabilized the quaternary structure. In vivo heterologous enzyme expression experiments in Escherichia coli revealed that GLP can protect bacteria against high concentrations of cyanide and hydrogen peroxide. Finally, phylogenetic analysis showed that homologous glp genes are distributed across Gram-negative bacterial families with conservation of the N- to C-domain order. However, no eukaryotic organism contains this enzyme. Altogether, these results suggest that GLP is an important enzyme with cyanide-decomposing and sulfurtransferase functions in bacteria, whose presence in eukaryotes we could not observe, representing a promising biological target for new pharmaceuticals.</div></front></TEI><pubmed><MedlineCitation Status="In-Process" Owner="NLM"><PMID Version="1">32307572</PMID><DateRevised><Year>2020</Year><Month>06</Month><Day>08</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1432-0614</ISSN><JournalIssue CitedMedium="Internet"><Volume>104</Volume><Issue>12</Issue><PubDate><Year>2020</Year><Month>Jun</Month></PubDate></JournalIssue><Title>Applied microbiology and biotechnology</Title><ISOAbbreviation>Appl Microbiol Biotechnol</ISOAbbreviation></Journal><ArticleTitle>Glutaredoxin-like protein (GLP)-a novel bacteria sulfurtransferase that protects cells against cyanide and oxidative stresses.</ArticleTitle><Pagination><MedlinePgn>5477-5492</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1007/s00253-020-10491-5</ELocationID><Abstract><AbstractText>The pathogen Xylella fastidiosa belongs to the Xanthomonadaceae family, a large group of Gram-negative bacteria that cause diseases in many economically important crops. A predicted gene, annotated as glutaredoxin-like protein (glp), was found to be highly conserved among the genomes of different genera within this family and highly expressed in X. fastidiosa. Analysis of the GLP protein sequences revealed three protein domains: one similar to monothiol glutaredoxins (Grx), an Fe-S cluster and a thiosulfate sulfurtransferase/rhodanese domain (Tst/Rho), which is generally involved in sulfur metabolism and cyanide detoxification. To characterize the biochemical properties of GLP, we expressed and purified the X. fastidiosa recombinant GLP enzyme. Grx activity and Fe-S cluster formation were not observed, while an evaluation of Tst/Rho enzymatic activity revealed that GLP can detoxify cyanide and transfer inorganic sulfur to acceptor molecules in vitro. The biological activity of GLP relies on the cysteine residues in the Grx and Tst/Rho domains (Cys<sup>33</sup> and Cys<sup>266</sup>, respectively), and structural analysis showed that GLP and GLP<sup>C266S</sup> were able to form high molecular weight oligomers (> 600 kDa), while replacement of Cys<sup>33</sup> with Ser destabilized the quaternary structure. In vivo heterologous enzyme expression experiments in Escherichia coli revealed that GLP can protect bacteria against high concentrations of cyanide and hydrogen peroxide. Finally, phylogenetic analysis showed that homologous glp genes are distributed across Gram-negative bacterial families with conservation of the N- to C-domain order. However, no eukaryotic organism contains this enzyme. Altogether, these results suggest that GLP is an important enzyme with cyanide-decomposing and sulfurtransferase functions in bacteria, whose presence in eukaryotes we could not observe, representing a promising biological target for new pharmaceuticals.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>de Paula</LastName><ForeName>Carla Peres</ForeName><Initials>CP</Initials><AffiliationInfo><Affiliation>Laboratory of Structural Molecular Biology, Biosciences Institute, UNESP - São Paulo State University, São Vicente, SP, Brazil.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Dos Santos</LastName><ForeName>Melina Cardoso</ForeName><Initials>MC</Initials><AffiliationInfo><Affiliation>Laboratory of Structural Molecular Biology, Biosciences Institute, UNESP - São Paulo State University, São Vicente, SP, Brazil.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Tairum</LastName><ForeName>Carlos A</ForeName><Initials>CA</Initials><AffiliationInfo><Affiliation>Laboratory of Structural Molecular Biology, Biosciences Institute, UNESP - São Paulo State University, São Vicente, SP, Brazil.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Breyer</LastName><ForeName>Carlos Alexandre</ForeName><Initials>CA</Initials><AffiliationInfo><Affiliation>Laboratory of Structural Molecular Biology, Biosciences Institute, UNESP - São Paulo State University, São Vicente, SP, Brazil.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Toledo-Silva</LastName><ForeName>Guilherme</ForeName><Initials>G</Initials><AffiliationInfo><Affiliation>Laboratory of Biomarkers of Aquatic Contamination and Immunochemistry, Department of Biochemistry, Federal University of Santa Catarina, Florianopolis, SC, Brazil.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Toyama</LastName><ForeName>Marcos Hikari</ForeName><Initials>MH</Initials><AffiliationInfo><Affiliation>Laboratory of Functional and Structural Characterization of Toxins of Venomous and Poisonous Animals, Biosciences Institute, UNESP - São Paulo State University, São Vicente, SP, Brazil.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Mori</LastName><ForeName>Gustavo Maruyama</ForeName><Initials>GM</Initials><AffiliationInfo><Affiliation>Molecular Ecology Laboratory, Biosciences Institute, UNESP - São Paulo State University, São Vicente, SP, Brazil.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>de Oliveira</LastName><ForeName>Marcos Antonio</ForeName><Initials>MA</Initials><AffiliationInfo><Affiliation>Laboratory of Structural Molecular Biology, Biosciences Institute, UNESP - São Paulo State University, São Vicente, SP, Brazil. mao@clp.unesp.br.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>2007/50930-3</GrantID><Agency>Fundação de Amparo à Pesquisa do Estado de São Paulo</Agency><Country></Country></Grant><Grant><GrantID>2017/19942-7</GrantID><Agency>Fundação de Amparo à Pesquisa do Estado de São Paulo</Agency><Country></Country></Grant><Grant><GrantID>2017/20291-0</GrantID><Agency>Fundação de Amparo à Pesquisa do Estado de São Paulo</Agency><Country></Country></Grant><Grant><GrantID>10/16827-3</GrantID><Agency>Fundação de Amparo à Pesquisa do Estado de São Paulo</Agency><Country></Country></Grant><Grant><GrantID>2013/16192-6</GrantID><Agency>Fundação de Amparo à Pesquisa do Estado de São Paulo</Agency><Country></Country></Grant><Grant><GrantID>10/00172-8</GrantID><Agency>Fundação de Amparo à Pesquisa do Estado de São Paulo</Agency><Country></Country></Grant><Grant><GrantID>2011/13500-6</GrantID><Agency>Fundação de Amparo à Pesquisa do Estado de São Paulo</Agency><Country></Country></Grant><Grant><GrantID>2013/07937-8</GrantID><Agency>FAPESP - Redox Processes in Biomedicine</Agency><Country></Country></Grant><Grant><GrantID>2013/16192-6</GrantID><Agency>FAPESP</Agency><Country></Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2020</Year><Month>04</Month><Day>19</Day></ArticleDate></Article><MedlineJournalInfo><Country>Germany</Country><MedlineTA>Appl Microbiol Biotechnol</MedlineTA><NlmUniqueID>8406612</NlmUniqueID><ISSNLinking>0175-7598</ISSNLinking></MedlineJournalInfo><CitationSubset>IM</CitationSubset><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Glutaredoxin (Grx)</Keyword><Keyword MajorTopicYN="N">Glutaredoxin-like protein (GLP)</Keyword><Keyword MajorTopicYN="N">Reactive oxygen species (ROS)</Keyword><Keyword MajorTopicYN="N">Thiosulfate sulfurtransferase/Rhodanese (Tst/Rho)</Keyword><Keyword MajorTopicYN="N">Xylella fastidiosa</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2019</Year><Month>10</Month><Day>27</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2020</Year><Month>02</Month><Day>20</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2020</Year><Month>02</Month><Day>14</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2020</Year><Month>4</Month><Day>21</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>4</Month><Day>21</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2020</Year><Month>4</Month><Day>21</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">32307572</ArticleId><ArticleId IdType="doi">10.1007/s00253-020-10491-5</ArticleId><ArticleId IdType="pii">10.1007/s00253-020-10491-5</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Brésil</li></country><region><li>Santa Catarina</li><li>État de São Paulo</li></region></list><tree><country name="Brésil"><region name="État de São Paulo"><name sortKey="De Paula, Carla Peres" sort="De Paula, Carla Peres" uniqKey="De Paula C" first="Carla Peres" last="De Paula">Carla Peres De Paula</name></region><name sortKey="Breyer, Carlos Alexandre" sort="Breyer, Carlos Alexandre" uniqKey="Breyer C" first="Carlos Alexandre" last="Breyer">Carlos Alexandre Breyer</name><name sortKey="De Oliveira, Marcos Antonio" sort="De Oliveira, Marcos Antonio" uniqKey="De Oliveira M" first="Marcos Antonio" last="De Oliveira">Marcos Antonio De Oliveira</name><name sortKey="Dos Santos, Melina Cardoso" sort="Dos Santos, Melina Cardoso" uniqKey="Dos Santos M" first="Melina Cardoso" last="Dos Santos">Melina Cardoso Dos Santos</name><name sortKey="Mori, Gustavo Maruyama" sort="Mori, Gustavo Maruyama" uniqKey="Mori G" first="Gustavo Maruyama" last="Mori">Gustavo Maruyama Mori</name><name sortKey="Tairum, Carlos A" sort="Tairum, Carlos A" uniqKey="Tairum C" first="Carlos A" last="Tairum">Carlos A. Tairum</name><name sortKey="Toledo Silva, Guilherme" sort="Toledo Silva, Guilherme" uniqKey="Toledo Silva G" first="Guilherme" last="Toledo-Silva">Guilherme Toledo-Silva</name><name sortKey="Toyama, Marcos Hikari" sort="Toyama, Marcos Hikari" uniqKey="Toyama M" first="Marcos Hikari" last="Toyama">Marcos Hikari Toyama</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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