RAP, the Sole Octotricopeptide Repeat Protein in Arabidopsis, Is Required for Chloroplast 16S rRNA Maturation. Issue 2 (28th February 2014)
- Record Type:
- Journal Article
- Title:
- RAP, the Sole Octotricopeptide Repeat Protein in Arabidopsis, Is Required for Chloroplast 16S rRNA Maturation. Issue 2 (28th February 2014)
- Main Title:
- RAP, the Sole Octotricopeptide Repeat Protein in Arabidopsis, Is Required for Chloroplast 16S rRNA Maturation
- Authors:
- Kleinknecht, Laura
Wang, Fei
Stübe, Roland
Philippar, Katrin
Nickelsen, Jörg
Bohne, Alexandra-Viola - Abstract:
- Abstract : Chloroplast gene expression is mainly regulated by nucleus-encoded helical repeat proteins, like PPR, TPR, and OPR proteins. This study identifies a molecular role for RAP, the only OPR protein in Arabidopsis, in chloroplast 16S rRNA maturation. Furthermore, it provides evidence that the nucleoid is the relevant suborganellar location for rRNA maturation in the chloroplast. Abstract: The biogenesis and activity of chloroplasts in both vascular plants and algae depends on an intracellular network of nucleus-encoded, trans -acting factors that control almost all aspects of organellar gene expression. Most of these regulatory factors belong to the helical repeat protein superfamily, which includes tetratricopeptide repeat, pentatricopeptide repeat, and the recently identified octotricopeptide repeat (OPR) proteins. Whereas green algae express many different OPR proteins, only a single orthologous OPR protein is encoded in the genomes of most land plants. Here, we report the characterization of the only OPR protein in Arabidopsis thaliana, RAP, which has previously been implicated in plant pathogen defense. Loss of RAP led to a severe defect in processing of chloroplast 16S rRNA resulting in impaired chloroplast translation and photosynthesis. In vitro RNA binding and RNase protection assays revealed that RAP has an intrinsic and specific RNA binding capacity, and the RAP binding site was mapped to the 5′ region of the 16S rRNA precursor. Nucleoid localization of RAPAbstract : Chloroplast gene expression is mainly regulated by nucleus-encoded helical repeat proteins, like PPR, TPR, and OPR proteins. This study identifies a molecular role for RAP, the only OPR protein in Arabidopsis, in chloroplast 16S rRNA maturation. Furthermore, it provides evidence that the nucleoid is the relevant suborganellar location for rRNA maturation in the chloroplast. Abstract: The biogenesis and activity of chloroplasts in both vascular plants and algae depends on an intracellular network of nucleus-encoded, trans -acting factors that control almost all aspects of organellar gene expression. Most of these regulatory factors belong to the helical repeat protein superfamily, which includes tetratricopeptide repeat, pentatricopeptide repeat, and the recently identified octotricopeptide repeat (OPR) proteins. Whereas green algae express many different OPR proteins, only a single orthologous OPR protein is encoded in the genomes of most land plants. Here, we report the characterization of the only OPR protein in Arabidopsis thaliana, RAP, which has previously been implicated in plant pathogen defense. Loss of RAP led to a severe defect in processing of chloroplast 16S rRNA resulting in impaired chloroplast translation and photosynthesis. In vitro RNA binding and RNase protection assays revealed that RAP has an intrinsic and specific RNA binding capacity, and the RAP binding site was mapped to the 5′ region of the 16S rRNA precursor. Nucleoid localization of RAP was shown by transient green fluorescent protein import assays, implicating the nucleoid as the site of chloroplast rRNA processing. Taken together, our data indicate that the single OPR protein in Arabidopsis is important for a basic process of chloroplast biogenesis. … (more)
- Is Part Of:
- The Plant Cell. Volume 26:Issue 2(2014)
- Journal:
- The Plant Cell
- Issue:
- Volume 26:Issue 2(2014)
- Issue Display:
- Volume 26, Issue 2 (2014)
- Year:
- 2014
- Volume:
- 26
- Issue:
- 2
- Issue Sort Value:
- 2014-0026-0002-0000
- Page Start:
- 777
- Page End:
- 787
- Publication Date:
- 2014-02-28
- Journal URLs:
- http://www.oxfordjournals.org/ ↗
- DOI:
- 10.1105/tpc.114.122853 ↗
- Languages:
- English
- ISSNs:
- 1040-4651
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 16368.xml