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Título: | Role of an intrasubunit disulfide in the association state of the cytosolic homo-oligomer methionine adenosyltransferase |
Autor: | Sánchez-Pérez, Gabino F.; Gasset, M. CSIC ORCID; Calvete, Juan J. CSIC ORCID; Pajares, María A. CSIC ORCID | Fecha de publicación: | 2003 | Editor: | American Society for Biochemistry and Molecular Biology | Citación: | Journal of Biological Chemistry 278(9): 7285-7293 (2003) | Resumen: | Recombinant rat liver methionine adenosyltransferase has been refolded into fully active tetramers (MAT I) and dimers (MAT III), using as a source chaotrope-solubilized aggregates resulting from specific washes of inclusion bodies. The conditions of refolding, dialysis in the presence of 10 mM dithiothreitol or 10 mM GSH with I mM GSSG, allowed the production of both isoforms, the nature of the redox agent determining the capacity of the final product (MAT I/III) to interconvert. Refolding in the presence of 10 mM dithiothreitol yielded mainly MAT III in a concentration-dependent equilibrium with the homotetramer MAT I. However, refolding in the presence of the redox pair GSH/GSSG resulted in a stable MAT I and III mixture. Blockage of dimer-tetramer interconversion has been found related to the production of a single intramolecular disulfide in methionine adenosyltransferase during the GSH/GSSG folding process. The residues involved in this disulfide have been identified by mass spectrometry and using a set of single cysteine mutants as cysteines 35 and 61. In addition, a kinetic intermediate in the MAT I dissociation to MAT III has been detected. The physiological importance of these results is discussed in light of the structural and regulatory data available. | Versión del editor: | https://doi.org/10.1074/jbc.M210177200 | URI: | http://hdl.handle.net/10261/80143 | DOI: | 10.1074/jbc.M210177200 | Identificadores: | doi: 10.1074/jbc.M210177200 issn: 0021-9258 e-issn: 1083-351X |
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