RRC ID 35513
Author Santos CA, Toledo MA, Trivella DB, Beloti LL, Schneider DR, Saraiva AM, Crucello A, Azzoni AR, Souza AA, Aparicio R, Souza AP.
Title Functional and structural studies of the disulfide isomerase DsbC from the plant pathogen Xylella fastidiosa reveals a redox-dependent oligomeric modulation in vitro.
Journal FEBS J.
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.
Volume 279(20)
Pages 3828-43
Published 2012-10
DOI 10.1111/j.1742-4658.2012.08743.x
PMID 22889056
MeSH Amino Acid Sequence Bacterial Proteins / chemistry* Bacterial Proteins / genetics Bacterial Proteins / metabolism Biofilms / drug effects Biofilms / growth & development Copper / pharmacology Escherichia coli / enzymology Escherichia coli / genetics Escherichia coli / growth & development Genetic Complementation Test Models, Molecular Molecular Sequence Data Mutation Oxidation-Reduction Plant Diseases / microbiology Protein Disulfide-Isomerases / chemistry* Protein Disulfide-Isomerases / genetics Protein Disulfide-Isomerases / metabolism Protein Multimerization* Protein Structure, Quaternary Scattering, Small Angle Sequence Homology, Amino Acid X-Ray Diffraction Xylella / enzymology* Xylella / genetics Xylella / physiology
IF 4.739
Times Cited 3
Prokaryotes E. coli JW2861(ASKA library) ME9062(BW25113)