| Texto completo | |
| Autor(es): Mostrar menos - |
Santos, Clelton A.
[1]
;
Toledo, Marcelo A. S.
[1]
;
Trivella, Daniela B. B.
[2]
;
Beloti, Lilian L.
[1]
;
Schneider, Dilaine R. S.
[1]
;
Saraiva, Antonio M.
[1]
;
Crucello, Aline
[1]
;
Azzoni, Adriano R.
[1, 3]
;
Souza, Alessandra A.
[4]
;
Aparicio, Ricardo
[2]
;
Souza, Anete P.
[1, 5]
Número total de Autores: 11
|
| Afiliação do(s) autor(es): | [1] Univ Estadual Campinas, CBMEG, BR-13083875 Campinas, SP - Brazil
[2] Univ Estadual Campinas, Inst Quim, Lab Biol Estrutural & Cristalog, BR-13083875 Campinas, SP - Brazil
[3] Univ Sao Paulo, Escola Politecn, Dept Engn Quim, BR-05508 Sao Paulo - Brazil
[4] Ctr APTA Citros Sylvio Moreira IAC, Cordeiropolis - Brazil
[5] Univ Estadual Campinas, Dept Biol Vegetal, Inst Biol, BR-13083875 Campinas, SP - Brazil
Número total de Afiliações: 5
|
| Tipo de documento: | Artigo Científico |
| Fonte: | FEBS Journal; v. 279, n. 20, p. 3828-3843, OCT 2012. |
| Citações Web of Science: | 3 |
| Resumo | |
Xylella fastidiosa is a Gram-negative bacterium that grows as a biofilm inside the xylem vessels of susceptible plants and causes several economically relevant crop diseases. In the present study, we report the functional and low-resolution structural characterization of the X. fastidiosa disulfide isomerase DsbC (XfDsbC). DsbC is part of the disulfide bond reduction/isomerization pathway in the bacterial periplasm and plays an important role in oxidative protein folding. In the present study, we demonstrate the presence of XfDsbC during different stages of X. fastidiosa biofilm development. XfDsbC was not detected during X. fastidiosa planktonic growth; however, after administering a sublethal copper shock, we observed an overexpression of XfDsbC that also occurred during planktonic growth. These results suggest that X. fastidiosa can use XfDsbC in vivo under oxidative stress conditions similar to those induced by copper. In addition, using dynamic light scattering and small-angle X-ray scattering, we observed that the oligomeric state of XfDsbC in vitro may be dependent on the redox environment. Under reducing conditions, XfDsbC is present as a dimer, whereas a putative tetrameric form was observed under nonreducing conditions. Taken together, our findings demonstrate the overexpression of XfDsbC during biofilm formation and provide the first structural model of a bacterial disulfide isomerase in solution. Structured digital abstract XfDsbC and XfDsbC bind by x ray scattering (View Interaction: 1, 2) XfDsbC and XfDsbC bind by molecular sieving (View interaction) XfDsbC and XfDsbC bind by comigration in non denaturing gel electrophoresis (View interaction) XfDsbC and XfDsbC bind by cross-linking study (View Interaction: 1, 2) XfDsbC and XfDsbC bind by dynamic light scattering (View Interaction: 1, 2) (AU) | |
| Processo FAPESP: | 01/07533-7 - Resolução da estrutura tridimensional de proteínas relacionadas à patogenicidade de Xyllela fastidiosa |
| Beneficiário: | Anete Pereira de Souza |
| Modalidade de apoio: | Auxílio à Pesquisa - Regular |
| Processo FAPESP: | 08/55690-3 - Expressão, purificação e caracterização estrutural e funcional de proteínas relacionadas à patogenicidade de Xylella fastidiosa |
| Beneficiário: | Clelton Aparecido dos Santos |
| Modalidade de apoio: | Bolsas no Brasil - Doutorado |