The non-catalytic N-terminal domain of ACS7 is involved in the post-translational regulation of this gene in Arabidopsis
© The Author 2014. Published by Oxford University Press on behalf of the Society for Experimental Biology. All rights reserved. For permissions, please email: journals.permissionsoup.com.
| Veröffentlicht in: | Journal of experimental botany. - 1985. - 65(2014), 15 vom: 15. Aug., Seite 4397-408 |
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| Weitere Verfasser: | , , , |
| Format: | Online-Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2014
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| Zugriff auf das übergeordnete Werk: | Journal of experimental botany |
| Schlagworte: | Journal Article Research Support, Non-U.S. Gov't 1-Aminocyclopropane-1-carboxylate synthase 7 Arabidopsis N-terminus ethylene post-translational regulation protein stability. Proteasome Endopeptidase Complex EC 3.4.25.1 mehr... |
| Zusammenfassung: | © The Author 2014. Published by Oxford University Press on behalf of the Society for Experimental Biology. All rights reserved. For permissions, please email: journals.permissionsoup.com. Post-transcriptional control of the expression of the 1-aminocyclopropane-1-carboxylate synthase (ACS) gene family is important for maintaining appropriate levels of ethylene production. However, the molecular mechanism underlying the post-transcriptional regulation of type 3 ACS proteins remains unclear. Multiple sequence alignment revealed that the N-terminus of type 3 ACSs was longer than that of other ACSs. Fusing the N-terminal 54 residues of ACS7, the sole type 3 ACS in Arabidopsis, to the β-glucuronidase (GUS) reporter significantly decreased the stability of N(7(1-54))-GUS fusion protein. Among these 54 residues, residues 1-14 conferred this negative effect on the GUS fusion gene. Consistently, a truncated form of ACS7 lacking residues 1-14 was more stable than full-length ACS7 when transgenically expressed in Arabidopsis and led to a more severe ethylene response phenotype in the light-grown transgenic seedlings. Interestingly, the ACS7 N-terminus had no effect on the stability of N(7)-GUS and ACS7 proteins at the etiolated seedling stage. Both exogenous 1-aminocyclopropane-1-carboxylic acid (ACC) treatment and salt stress could rescue the levels of accumulation of N(7)-GUS fusion protein in light-grown seedlings. These results suggest that the non-catalytic N-terminus of ACS7 is involved in its own post-translational regulation. The proteasome inhibitor MG132 suppressed degradation of full-length ACS7 in vivo, but had little effect on the N-terminal truncated form of ACS7, indicating that the N-terminus mediates the regulation of ACS7 stability through the ubiquitin-26S proteasome pathway |
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| Beschreibung: | Date Completed 01.04.2015 Date Revised 29.07.2014 published: Print-Electronic Citation Status MEDLINE |
| ISSN: | 1460-2431 |
| DOI: | 10.1093/jxb/eru211 |