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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Biochemical and biophysical characterization of a mycoredoxin protein glutaredoxin A1 from Corynebacterium pseudotuberculosis

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Author(s):
Eberle, Raphael J. [1] ; Kawai, Liege A. [1] ; de Moraes, Fabio R. [1] ; Tasic, Ljubica [2] ; Arni, Raghuvir K. [1] ; Coronado, Monika A. [1]
Total Authors: 6
Affiliation:
[1] UNESP, Ibilce, Dept Phys, Multiuser Ctr Biomol Innovat, Rua Cristovao Colombo 2265, BR-15054000 Sao Jose Do Rio Preto, SP - Brazil
[2] Univ Estadual Campinas, Inst Chem, BR-13083970 Campinas, SP - Brazil
Total Affiliations: 2
Document type: Journal article
Source: International Journal of Biological Macromolecules; v. 107, n. B, p. 1999-2007, FEB 2018.
Web of Science Citations: 1
Abstract

Glutaredoxin A1 from Corynebacterium pseudotuberculosis was shown to be a mycoredoxin protein. In this study, we established a process to overexpress and purify glutaredoxin A1. The aim of this study was the investigation of the Glutaredoxin A1 from C pseudotuberculosis behavior under different redox environments and the identification of lead molecules, which can be used for specific inhibitor development for this protein family. A quantitative assay was performed measuring the rate of insulin reduction spectrophotometrically at 640 nm through turbidity formation from the precipitation of the free insulin. Glutaredoxin A1, at 5 mu M concentration, accelerated the reduction process of 0.2 mM insulin and 1 mM DTT. The pH optimum of the reaction was 7.4. In the presence of DTT and ESH the glutaredoxin A1 presents similar activity, and its activity is reduced by 50% in the presence of GSH. Additional function for ESH in the redox metabolism of C. pseudotuberculosis is suggested. A combined STD and Chemical Shift - NMR approach was employed to study the effects of potential inhibitors on the structure of glutaredoxin A1 from Corynebacterium pseudotuberculosis. The inhibitory potential of four ligands (heparin, suramin, hesperetin - Hst, and hesperidin - Hsp) against glutaredoxin A1 is discussed. (C) 2017 Elsevier B.V. All rights reserved. (AU)

FAPESP's process: 16/08104-8 - Structural and functional aspects of two DNA binding proteins encoded by Corynebacterium pseudotuberculosis
Grantee:Raphael Josef Eberle
Support type: Scholarships in Brazil - Post-Doctorate
FAPESP's process: 15/13765-0 - Structural Studies and Characterization of Proteins by X-ray Crystallography and Nuclear Magnetic Resonance. Structural investigations and biophysics of molecular mechanisms of functional proteins.
Grantee:Raghuvir Krishnaswamy Arni
Support type: Regular Research Grants
FAPESP's process: 09/53989-4 - Acquisition of a nuclear magnetic resonance spectrometer for studies of biomolecules
Grantee:Raghuvir Krishnaswamy Arni
Support type: Multi-user Equipment Program
FAPESP's process: 16/12904-0 - Mechanism and Molecular Interactions of Bioactive molecules with NS3 protease from Zika virus.
Grantee:Monika Aparecida Coronado
Support type: Scholarships in Brazil - Post-Doctorate
FAPESP's process: 15/18868-2 - Multi-user equipment acquisition for molecular and structural biology
Grantee:Raghuvir Krishnaswamy Arni
Support type: Multi-user Equipment Program