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231224s2015 xx |||||o 00| ||eng c |
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|a 10.1093/jxb/erv286
|2 doi
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|a pubmed24n0833.xml
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|a (DE-627)NLM250066947
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|a (NLM)26085677
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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| 100 |
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|a Wei, Jia
|e verfasserin
|4 aut
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| 245 |
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|a The E3 ligase AtCHIP positively regulates Clp proteolytic subunit homeostasis
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|c 2015
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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|a Date Completed 14.07.2016
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|a Date Revised 19.11.2018
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a © The Author 2015. 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 The caseinolytic peptidase (Clp) core proteins are essential for plant growth and development, especially for chloroplast function. Antisense or overexpression of ClpP4, which is one of the Clp core subunits, causes chlorotic phenotypes in Arabidopsis. An E3 ligase gene, AtCHIP, has previously been found to ubiquitylate ClpP4 in vitro. ClpP4 antisense and overexpressing plants that also overexpressed AtCHIP were constructed to explore the effect of AtCHIP on ClpP4. Overexpression of AtCHIP was found to rescue the chlorotic phenotypes of both ClpP4 antisense and overexpressing plants. The unbalanced levels of Clp core proteins in ClpP4 antisense and overexpressing plants with overexpression of AtCHIP were similar to wild-type levels, suggesting that AtCHIP regulates Clp core proteins. The results also show that AtCHIP can interact with ClpP3 and ClpP5 in yeast and ubiquitylate ClpP3 and ClpP5 in vitro. This suggests that AtCHIP is directly related to ClpP3 and ClpP5. Given these results, the inference is that through selective degradation of Clp subunits, AtCHIP could positively regulate homeostasis of Clp proteolytic subunits and maximize the production of functional chloroplasts. Similar results were obtained from transgenic tobacco plants, suggesting that regulation of the Clp protease by AtCHIP is conserved
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a AtCHIP
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|a Clp proteolytic subunits
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|a ClpP3
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|a ClpP4
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|a ClpP5
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|a chloroplast protease
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|a protein homeostasis.
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|a Arabidopsis Proteins
|2 NLM
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|a Ubiquitin
|2 NLM
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|a CHIP protein, Arabidopsis
|2 NLM
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| 650 |
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|a EC 2.3.2.27
|2 NLM
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| 650 |
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|a Ubiquitin-Protein Ligases
|2 NLM
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| 650 |
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|a EC 2.3.2.27
|2 NLM
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| 650 |
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|a Endopeptidase Clp
|2 NLM
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| 650 |
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|a EC 3.4.21.92
|2 NLM
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| 700 |
1 |
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|a Qiu, Xiaoyun
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Chen, Lin
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Hu, Wenjun
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Hu, Rongbin
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Chen, Jian
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Sun, Li
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Li, Li
|e verfasserin
|4 aut
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| 700 |
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|a Zhang, Hong
|e verfasserin
|4 aut
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| 700 |
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|a Lv, Zhiqiang
|e verfasserin
|4 aut
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| 700 |
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|a Shen, Guoxin
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Journal of experimental botany
|d 1985
|g 66(2015), 19 vom: 17. Sept., Seite 5809-20
|w (DE-627)NLM098182706
|x 1460-2431
|7 nnns
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| 773 |
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|g volume:66
|g year:2015
|g number:19
|g day:17
|g month:09
|g pages:5809-20
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|u http://dx.doi.org/10.1093/jxb/erv286
|3 Volltext
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|d 66
|j 2015
|e 19
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|c 09
|h 5809-20
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