A redox-sensitive cysteine residue regulates the kinase activities of OsMPK3 and OsMPK6 in vitro
Copyright © 2014 Elsevier Ireland Ltd. All rights reserved.
| Veröffentlicht in: | Plant science : an international journal of experimental plant biology. - 1985. - 227(2014) vom: 07. Okt., Seite 69-75 |
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| Format: | Online-Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2014
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| Zugriff auf das übergeordnete Werk: | Plant science : an international journal of experimental plant biology |
| Schlagworte: | Journal Article Research Support, Non-U.S. Gov't In vitro kinase activity MAPK Redox-control Rice Site-directed mutagenesis Plant Proteins Hydrogen Peroxide BBX060AN9V mehr... |
| Zusammenfassung: | Copyright © 2014 Elsevier Ireland Ltd. All rights reserved. Two subgroup A rice mitogen-activated protein kinases (MAPKs), OsMPK3 and OsMPK6, have been implicated in multiple stress responses. However, the redox-control of the kinase activity of these proteins remains unknown. Here, immunoprecipitated OsMPK3 and OsMPK6 were initially activated in 15min, and this activation transiently increased in rice seedlings under H2O2 stress. Among the six conserved cysteine residues, only the fourth cysteine residues in the kinase domain VII, Cys(179) and Cys(210), were required for the in vitro kinase activities of OsMPK3 and OsMPK6, respectively. Moreover, the substitution of these specific cysteine residues with serine abrogated in vitro kinase responses to redox conditions. These results suggest a novel redox-control mechanism for the kinase activities of these MAPKs in vivo |
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| Beschreibung: | Date Completed 18.05.2015 Date Revised 30.09.2020 published: Print-Electronic Citation Status MEDLINE |
| ISSN: | 1873-2259 |
| DOI: | 10.1016/j.plantsci.2014.07.002 |