A Redox 2-Cys mechanism regulates the catalytic activity of divergent Cyclophilins
| Autor(a) principal: | |
|---|---|
| Data de Publicação: | 2013 |
| Outros Autores: | , , , , , , , , , , |
| Tipo de documento: | Artigo |
| Idioma: | por |
| Título da fonte: | Repositório Institucional da FIOCRUZ (ARCA) |
| Texto Completo: | https://www.arca.fiocruz.br/handle/icict/15598 |
Resumo: | This work was supported by the Fundação de Amparo à Pesquisa do Estado de São Paulo (fellowship to B.M.C.) and the Conselho Nacional de Desenvolvimento Científico e Tecnológico. |
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Campos, Bruna MedéiaSforça, Mauricio LuisAmbrosio, Andre Luis BerteliDomingues, Mariane NoronhaSouza, Tatiana de Arruda Campos Brasil deBarbosa, João Alexandre Ribeiro GonçalvezLeme, Adriana Franco PaesPerez, Carlos AlbertoWhittaker, Sara Britt-MarieMurakami, Mario TyagoZer, Ana Carolina de MatosBenedetti, Celso Eduardo2016-09-02T17:03:14Z2016-09-02T17:03:14Z2013CAMPOS, Bruna Medéia et al. A Redox 2-Cys mechanism regulates the catalytic activity of divergent Cyclophilins. Plant Physiol. v. 162, n. 3, p. 1311-1323, 2013.0032-0889https://www.arca.fiocruz.br/handle/icict/1559810.1104/pp.113.218339.This work was supported by the Fundação de Amparo à Pesquisa do Estado de São Paulo (fellowship to B.M.C.) and the Conselho Nacional de Desenvolvimento Científico e Tecnológico.Centro Nacional de Pesquisa em Energia e Materiais. Laboratório Nacional de Biociências. Campinas, SP, Brasil.Centro Nacional de Pesquisa em Energia e Materiais. Laboratório Nacional de Biociências. Campinas, SP, Brasil.Centro Nacional de Pesquisa em Energia e Materiais. Laboratório Nacional de Biociências. Campinas, SP, Brasil.Centro Nacional de Pesquisa em Energia e Materiais. Laboratório Nacional de Biociências. Campinas, SP, Brasil.Centro Nacional de Pesquisa em Energia e Materiais. Laboratório Nacional de Biociências. Campinas, SP, Brasil. / Fundação Oswaldo Cruz. Instituto Carlos Chagas. Curitiba, PR, Brasil.Centro Nacional de Pesquisa em Energia e Materiais. Laboratório Nacional de Biociências. Campinas, SP, Brasil. / Universidade de Brasília. Instituto de Ciências Biológicas. Departamento de Biologia Celular. Brasília, DF, Brasil.Centro Nacional de Pesquisa em Energia e Materiais. Laboratório Nacional de Biociências. Campinas, SP, Brasil.Centro Nacional de Pesquisa em Energia e Materiais. Laboratório Nacional de Luz Síncrotron. Campinas, SP, Brasil.University of Birmingham. School of Cancer Sciences. Birmingham, United Kingdom.Centro Nacional de Pesquisa em Energia e Materiais. Laboratório Nacional de Biociências. Campinas, SP, Brasil.University of Birmingham. School of Cancer Sciences. Birmingham, United Kingdom.Centro Nacional de Pesquisa em Energia e Materiais. Laboratório Nacional de Biociências. Campinas, SP, Brasil.The citrus (Citrus sinensis) cyclophilin CsCyp is a target of the Xanthomonas citri transcription activator-like effector PthA, required to elicit cankers on citrus. CsCyp binds the citrus thioredoxin CsTdx and the carboxyl-terminal domain of RNA polymerase II and is a divergent cyclophilin that carries the additional loop KSGKPLH, invariable cysteine (Cys) residues Cys-40 and Cys-168, and the conserved glutamate (Glu) Glu-83. Despite the suggested roles in ATP and metal binding, the functions of these unique structural elements remain unknown. Here, we show that the conserved Cys residues form a disulfide bond that inactivates the enzyme, whereas Glu-83, which belongs to the catalytic loop and is also critical for enzyme activity, is anchored to the divergent loop to maintain the active site open. In addition, we demonstrate that Cys-40 and Cys-168 are required for the interaction with CsTdx and that CsCyp binds the citrus carboxyl-terminal domain of RNA polymerase II YSPSAP repeat. Our data support a model where formation of the Cys-40-Cys-168 disulfide bond induces a conformational change that disrupts the interaction of the divergent and catalytic loops, via Glu-83, causing the active site to close. This suggests a new type of allosteric regulation in divergent cyclophilins, involving disulfide bond formation and a loop-displacement mechanism.porA Redox 2-Cys mechanism regulates the catalytic activity of divergent Cyclophilinsinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleRedox 2-Cys MechanismCyclophilinsXanthomonas citrivirus replicationCiclofilinasReplicação Viralinfo:eu-repo/semantics/openAccessreponame:Repositório Institucional da FIOCRUZ (ARCA)instname:Fundação Oswaldo Cruz (FIOCRUZ)instacron:FIOCRUZLICENSElicense.txtlicense.txttext/plain; charset=utf-83074https://www.arca.fiocruz.br/bitstream/icict/15598/1/license.txt0271fb68963c017aa933c7aff60379f4MD51ORIGINALA Redox 2-Cys Mechanism.pdfA Redox 2-Cys Mechanism.pdfapplication/pdf2006330https://www.arca.fiocruz.br/bitstream/icict/15598/2/A%20Redox%202-Cys%20Mechanism.pdf4d520f5a1046b02fd7ebbcdfe4aa2dccMD52TEXTA Redox 2-Cys Mechanism.pdf.txtA Redox 2-Cys Mechanism.pdf.txtExtracted 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| dc.title.pt_BR.fl_str_mv |
A Redox 2-Cys mechanism regulates the catalytic activity of divergent Cyclophilins |
| title |
A Redox 2-Cys mechanism regulates the catalytic activity of divergent Cyclophilins |
| spellingShingle |
A Redox 2-Cys mechanism regulates the catalytic activity of divergent Cyclophilins Campos, Bruna Medéia Redox 2-Cys Mechanism Cyclophilins Xanthomonas citri virus replication Ciclofilinas Replicação Viral |
| title_short |
A Redox 2-Cys mechanism regulates the catalytic activity of divergent Cyclophilins |
| title_full |
A Redox 2-Cys mechanism regulates the catalytic activity of divergent Cyclophilins |
| title_fullStr |
A Redox 2-Cys mechanism regulates the catalytic activity of divergent Cyclophilins |
| title_full_unstemmed |
A Redox 2-Cys mechanism regulates the catalytic activity of divergent Cyclophilins |
| title_sort |
A Redox 2-Cys mechanism regulates the catalytic activity of divergent Cyclophilins |
| author |
Campos, Bruna Medéia |
| author_facet |
Campos, Bruna Medéia Sforça, Mauricio Luis Ambrosio, Andre Luis Berteli Domingues, Mariane Noronha Souza, Tatiana de Arruda Campos Brasil de Barbosa, João Alexandre Ribeiro Gonçalvez Leme, Adriana Franco Paes Perez, Carlos Alberto Whittaker, Sara Britt-Marie Murakami, Mario Tyago Zer, Ana Carolina de Matos Benedetti, Celso Eduardo |
| author_role |
author |
| author2 |
Sforça, Mauricio Luis Ambrosio, Andre Luis Berteli Domingues, Mariane Noronha Souza, Tatiana de Arruda Campos Brasil de Barbosa, João Alexandre Ribeiro Gonçalvez Leme, Adriana Franco Paes Perez, Carlos Alberto Whittaker, Sara Britt-Marie Murakami, Mario Tyago Zer, Ana Carolina de Matos Benedetti, Celso Eduardo |
| author2_role |
author author author author author author author author author author author |
| dc.contributor.author.fl_str_mv |
Campos, Bruna Medéia Sforça, Mauricio Luis Ambrosio, Andre Luis Berteli Domingues, Mariane Noronha Souza, Tatiana de Arruda Campos Brasil de Barbosa, João Alexandre Ribeiro Gonçalvez Leme, Adriana Franco Paes Perez, Carlos Alberto Whittaker, Sara Britt-Marie Murakami, Mario Tyago Zer, Ana Carolina de Matos Benedetti, Celso Eduardo |
| dc.subject.en.pt_BR.fl_str_mv |
Redox 2-Cys Mechanism Cyclophilins Xanthomonas citri virus replication |
| topic |
Redox 2-Cys Mechanism Cyclophilins Xanthomonas citri virus replication Ciclofilinas Replicação Viral |
| dc.subject.decs.pt_BR.fl_str_mv |
Ciclofilinas Replicação Viral |
| description |
This work was supported by the Fundação de Amparo à Pesquisa do Estado de São Paulo (fellowship to B.M.C.) and the Conselho Nacional de Desenvolvimento Científico e Tecnológico. |
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2013 |
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2013 |
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2016-09-02T17:03:14Z |
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2016-09-02T17:03:14Z |
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info:eu-repo/semantics/publishedVersion |
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info:eu-repo/semantics/article |
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CAMPOS, Bruna Medéia et al. A Redox 2-Cys mechanism regulates the catalytic activity of divergent Cyclophilins. Plant Physiol. v. 162, n. 3, p. 1311-1323, 2013. |
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https://www.arca.fiocruz.br/handle/icict/15598 |
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0032-0889 |
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10.1104/pp.113.218339. |
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CAMPOS, Bruna Medéia et al. A Redox 2-Cys mechanism regulates the catalytic activity of divergent Cyclophilins. Plant Physiol. v. 162, n. 3, p. 1311-1323, 2013. 0032-0889 10.1104/pp.113.218339. |
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