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231225s2019 xx |||||o 00| ||eng c |
| 024 |
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|a 10.1111/nph.15578
|2 doi
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|a pubmed24n0967.xml
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|a (DE-627)NLM290271665
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|a (NLM)30393849
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|a DE-627
|b ger
|c DE-627
|e rakwb
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| 041 |
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|a eng
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| 100 |
1 |
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|a Ruwe, Hannes
|e verfasserin
|4 aut
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| 245 |
1 |
4 |
|a The E domain of CRR2 participates in sequence-specific recognition of RNA in plastids
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| 264 |
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1 |
|c 2019
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| 336 |
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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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| 500 |
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|a Date Completed 27.02.2020
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|a Date Revised 30.09.2020
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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| 520 |
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|a © 2018 The Authors. New Phytologist © 2018 New Phytologist Trust.
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|a Pentatricopeptide repeat (PPR) proteins are modular RNA-binding proteins involved in different aspects of RNA metabolism in organelles. PPR proteins of the PLS subclass often contain C-terminal domains that are important for their function, but the role of one of these domains, the E domain, is far from resolved. Here, we elucidate the role of the E domain in CRR2 in plastids. We identified a surprisingly large number of small RNAs that represent in vivo footprints of the Arabidopsis PLS-class PPR protein CRR2. An unexpectedly strong base conservation was found in the nucleotides aligned to the E domain. We used both in vitro and in vivo experiments to reveal the role of the E domain of CRR2. The E domain of CRR2 can be predictably altered to prefer different nucleotides in its RNA ligand, and position 5 of the E1-motif is biologically important for the PPR-RNA interaction. The 'code' of the E domain PPR motifs is different from that of P- and S-motifs. The findings presented here show that the E domain of CRR2 is involved in sequence-specific interaction with its RNA ligand and have implications for our ability to predict RNA targets for PLS-PPRs and their use as biotechnological tools to manipulate specific RNAs in vivo
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4 |
|a Journal Article
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| 650 |
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4 |
|a Research Support, Non-U.S. Gov't
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4 |
|a Arabidopsis
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| 650 |
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4 |
|a E domain
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| 650 |
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4 |
|a RNA footprints
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| 650 |
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4 |
|a RNA processing
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| 650 |
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4 |
|a pentatricopeptide repeat (PPR) proteins
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| 650 |
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7 |
|a AT3G46790 protein, Arabidopsis
|2 NLM
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| 650 |
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7 |
|a Arabidopsis Proteins
|2 NLM
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| 650 |
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7 |
|a Chloroplast Proteins
|2 NLM
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| 650 |
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7 |
|a RNA, Plant
|2 NLM
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| 650 |
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7 |
|a RNA-Binding Proteins
|2 NLM
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| 650 |
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7 |
|a pentatricopeptide repeat protein, Arabidopsis
|2 NLM
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| 650 |
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7 |
|a Glycine
|2 NLM
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| 650 |
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7 |
|a TE7660XO1C
|2 NLM
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| 700 |
1 |
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|a Gutmann, Bernard
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Schmitz-Linneweber, Christian
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Small, Ian
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Kindgren, Peter
|e verfasserin
|4 aut
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| 773 |
0 |
8 |
|i Enthalten in
|t The New phytologist
|d 1979
|g 222(2019), 1 vom: 05. Apr., Seite 218-229
|w (DE-627)NLM09818248X
|x 1469-8137
|7 nnns
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| 773 |
1 |
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|g volume:222
|g year:2019
|g number:1
|g day:05
|g month:04
|g pages:218-229
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| 856 |
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|u http://dx.doi.org/10.1111/nph.15578
|3 Volltext
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|a AR
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|d 222
|j 2019
|e 1
|b 05
|c 04
|h 218-229
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