Functional and small-angle X-ray scattering studies of a new stationary phase survival protein E (SurE) from Xylella fastidiosa- evidence of allosteric behaviour

The genome data of bacterium Xylella fastidiosa strain 9a5c has identified several orfs related to its phytopathogenic adaptation and survival. Among these genes, the surE codifies a survival protein E (XfSurE) whose function is not so well understood, but functional assays in Escherichia coli revea...

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Bibliographic Details
Published in:The FEBS journal 2009-11, Vol.276 (22), p.6751-6762
Main Authors: Saraiva, Antonio M, Reis, Marcelo A, Tada, Susely F, Rosselli-Murai, Luciana K, Schneider, Dilaine R.S, Pelloso, Alexandre C, Toledo, Marcelo A.S, Giles, Carlos, Aparicio, Ricardo, de Souza, Anete P
Format: Article
Language:English
Subjects:
allosteric behaviour
Allosteric Regulation
Bacteria
Bacterial Proteins - chemistry
Bacterial Proteins - metabolism
Biochemistry
Chromatography, Gel
Circular Dichroism
Escherichia coli
Genetics
Genomics
Protein Multimerization
Protein Structure, Secondary
Proteins
Scattering, Small Angle
small-angle X-ray scattering
stationary phase survival protein E (SurE)
SurE oligomeric state
X-Rays
Xylella - metabolism
Xylella fastidiosa
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Summary:The genome data of bacterium Xylella fastidiosa strain 9a5c has identified several orfs related to its phytopathogenic adaptation and survival. Among these genes, the surE codifies a survival protein E (XfSurE) whose function is not so well understood, but functional assays in Escherichia coli revealed nucleotidase and exopolyphosphate activity. In the present study, we report the XfSurE protein overexpression in E. coli and its purification. The overall secondary structure was analyzed by CD. Small-angle X-ray scattering and gel filtration techniques demonstrated that the oligomeric state of the protein in solution is a tetramer. In addition, functional kinetics experiments were carried out with several monophosphate nucleoside substrates and revealed a highly positive cooperativity. An allosteric mechanism involving torsion movements in solution is proposed to explain the cooperative behaviour of XfSurE. This is the first characterization of a SurE enzyme from a phytopathogen organism and, to our knowledge, the first solution structure of a SurE protein to be described.
ISSN:1742-464X
1742-4658
DOI:10.1111/j.1742-4658.2009.07390.x