Mechanism of 1-Cys type methionine sulfoxide reductase A regeneration by glutaredoxin

Title
Mechanism of 1-Cys type methionine sulfoxide reductase A regeneration by glutaredoxin
Author(s)
김화영김문정정재호[정재호]정지혜[정지혜]황광연[황광연]이공주[이공주]
Keywords
ESCHERICHIA-COLI; STRESS; THIOREDOXINS; RESISTANCE; EXPRESSION; PROTEINS; ENZYME
Issue Date
201502
Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
Citation
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.457, no.4, pp.567 - 571
Abstract
Glutaredoxin (Grx), a major redox regulator, can act as a reductant of methionine sulfoxide reductase A (MsrA). However, the biochemical mechanisms involved in MsrA activity regeneration by Grx remain largely unknown. In this study, we investigated the regeneration mechanism of 1-Cys type Clostridium oremlandii MsrA (cMsrA) lacking a resolving Cys residue in a Grx-dependent assay. Kinetic analysis showed that cMsrA could be reduced by both monothiol and dithiol Grxs as efficiently as by in vitro reductant dithiothreitol. Our data revealed that the catalytic Cys sulfenic acid intermediate is not glutathionylated in the presence of the substrate, and that Grx instead directly formed a complex with cMsrA. Mass spectrometry analysis identified a disulfide bond between the N-terminal catalytic Cys of the active site of Grx and the catalytic Cys of cMsrA. This mixed disulfide bond could be resolved by glutathione. Based on these findings, we propose a model for regeneration of 1-Cys type cMsrA by Grx that involves no glutathionylation on the catalytic Cys of cMsrA. This mechanism contrasts with that of the previously known 1-Cys type MsrB. (C) 2015 Elsevier Inc. All rights reserved.
URI
http://hdl.handle.net/YU.REPOSITORY/33508http://dx.doi.org/10.1016/j.bbrc.2015.01.025
ISSN
0006-291X
Appears in Collections:
의과대학 > 생화학.분자생물학교실 > Articles
의과대학 > 영상의학과학교실 > Articles
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