Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/200150
Type: Artigo de periódico
Title: Functional And Structural Studies Of The Disulfide Isomerase Dsbc From The Plant Pathogen Xylella Fastidiosa Reveals A Redox-dependent Oligomeric Modulation In Vitro.
Author: Santos, Clelton A
Toledo, Marcelo A S
Trivella, Daniela B B
Beloti, Lilian L
Schneider, Dilaine R S
Saraiva, Antonio M
Crucello, Aline
Azzoni, Adriano R
Souza, Alessandra A
Aparicio, Ricardo
Souza, Anete P
Abstract: 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.
Subject: Amino Acid Sequence
Bacterial Proteins
Biofilms
Copper
Escherichia Coli
Genetic Complementation Test
Models, Molecular
Molecular Sequence Data
Mutation
Oxidation-reduction
Plant Diseases
Protein Disulfide-isomerases
Protein Multimerization
Protein Structure, Quaternary
Scattering, Small Angle
Sequence Homology, Amino Acid
X-ray Diffraction
Xylella
Rights: fechado
Identifier DOI: 10.1111/j.1742-4658.2012.08743.x
Address: http://www.ncbi.nlm.nih.gov/pubmed/22889056
Date Issue: 2012
Appears in Collections:Artigos e Materiais de Revistas Científicas - Unicamp

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