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231224s2014 xx |||||o 00| ||eng c |
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|a 10.1093/jxb/eru211
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|a pubmed24n0795.xml
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|a DE-627
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|a eng
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|a Xiong, Li
|e verfasserin
|4 aut
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|a The non-catalytic N-terminal domain of ACS7 is involved in the post-translational regulation of this gene in Arabidopsis
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|c 2014
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
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|2 rdamedia
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|a ƒa Online-Ressource
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|a Date Completed 01.04.2015
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|a Date Revised 29.07.2014
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a © 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.
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|a 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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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a 1-Aminocyclopropane-1-carboxylate synthase 7
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|a Arabidopsis
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|a N-terminus
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|a ethylene
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|a post-translational regulation
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|a protein stability.
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|a Proteasome Endopeptidase Complex
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|a ATP dependent 26S protease
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|a EC 3.4.99.-
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|a Lyases
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|a 1-aminocyclopropanecarboxylate synthase
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|a EC 4.4.1.14
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|a Xiao, Dong
|e verfasserin
|4 aut
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|a Xu, Xinxin
|e verfasserin
|4 aut
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|a Guo, Zhaoxia
|e verfasserin
|4 aut
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|a Wang, Ning Ning
|e verfasserin
|4 aut
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|i Enthalten in
|t Journal of experimental botany
|d 1985
|g 65(2014), 15 vom: 15. Aug., Seite 4397-408
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|x 1460-2431
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|g volume:65
|g year:2014
|g number:15
|g day:15
|g month:08
|g pages:4397-408
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|u http://dx.doi.org/10.1093/jxb/eru211
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