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231224s2017 xx |||||o 00| ||eng c |
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|a 10.1093/jxb/erx066
|2 doi
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|a pubmed25n0901.xml
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|a (DE-627)NLM270576754
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|a (NLM)28369470
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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|a Moreno, Juan C
|e verfasserin
|4 aut
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| 245 |
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|a Generation and characterization of a collection of knock-down lines for the chloroplast Clp protease complex in tobacco
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|c 2017
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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| 338 |
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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|a Date Completed 13.07.2018
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|a Date Revised 13.12.2023
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|a published: Print
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|a Citation Status MEDLINE
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|a © The Author 2017. Published by Oxford University Press on behalf of the Society for Experimental Biology.
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|a Protein degradation in chloroplasts is carried out by a set of proteases that eliminate misfolded, damaged, or superfluous proteins. The ATP-dependent caseinolytic protease (Clp) is the most complex protease in plastids and has been implicated mainly in stromal protein degradation. In contrast, FtsH, a thylakoid membrane-associated metalloprotease, is believed to participate mainly in the degradation of thylakoidal proteins. To determine the role of specific Clp and FtsH subunits in plant growth and development, RNAi lines targeting at least one subunit of each Clp ring and FtsH were generated in tobacco. In addition, mutation of the translation initiation codon was employed to down-regulate expression of the plastid-encoded ClpP1 subunit. These protease lines cover a broad range of reductions at the transcript and protein levels of the targeted genes. A wide spectrum of phenotypes was obtained, including pigment deficiency, alterations in leaf development, leaf variegations, and impaired photosynthesis. When knock-down lines for the different protease subunits were compared, both common and specific phenotypes were observed, suggesting distinct functions of at least some subunits. Our work provides a well-characterized collection of knock-down lines for plastid proteases in tobacco and reveals the importance of the Clp protease in physiology and plant development
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Chloroplast
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|a Clp protease
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|a Nicotiana
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|a leaf development
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|a photosynthesis
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|a plastid
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|a protease
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|a protein degradation
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|a protein stability.
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|a tabacum
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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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| 650 |
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|a Metalloendopeptidases
|2 NLM
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| 650 |
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|a EC 3.4.24.-
|2 NLM
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| 700 |
1 |
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|a Tiller, Nadine
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Diez, Mercedes
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Karcher, Daniel
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Tillich, Michael
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Schöttler, Mark A
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Bock, Ralph
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Journal of experimental botany
|d 1985
|g 68(2017), 9 vom: 01. Apr., Seite 2199-2218
|w (DE-627)NLM098182706
|x 1460-2431
|7 nnns
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| 773 |
1 |
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|g volume:68
|g year:2017
|g number:9
|g day:01
|g month:04
|g pages:2199-2218
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|u http://dx.doi.org/10.1093/jxb/erx066
|3 Volltext
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