ORRM5, an RNA recognition motif-containing protein, has a unique effect on mitochondrial RNA editing

© The Author 2017. Published by Oxford University Press on behalf of the Society for Experimental Biology.

Bibliographische Detailangaben
Veröffentlicht in:Journal of experimental botany. - 1985. - 68(2017), 11 vom: 17. Mai, Seite 2833-2847
1. Verfasser: Shi, Xiaowen (VerfasserIn)
Weitere Verfasser: Castandet, Benoit, Germain, Arnaud, Hanson, Maureen R, Bentolila, Stéphane
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2017
Zugriff auf das übergeordnete Werk:Journal of experimental botany
Schlagworte:Journal Article Glycine-rich RNA editing mitochondria plant development plant editosome plant stress response Arabidopsis Proteins ORRM5 protein, Arabidopsis RNA, Mitochondrial mehr... RNA, Plant RNA-Binding Proteins RNA 63231-63-0
Beschreibung
Zusammenfassung:© The Author 2017. Published by Oxford University Press on behalf of the Society for Experimental Biology.
Plants have an RNA editing mechanism that prevents deleterious organelle mutations from resulting in impaired proteins. A typical flowering plant modifies about 40 cytidines in chloroplast transcripts and many hundreds of cytidines in mitochondrial transcripts. The plant editosome, the molecular machinery responsible for this process, contains members of several protein families, including the organelle RNA recognition motif (ORRM)-containing family. ORRM1 and ORRM6 are chloroplast editing factors, while ORRM2, ORRM3, and ORRM4 are mitochondrial editing factors. Here we report the identification of organelle RRM protein 5 (ORRM5) as a mitochondrial editing factor with a unique mode of action. Unlike other ORRM editing factors, the absence of ORRM5 in orrm5 mutant plants results in an increase of the editing extent in 14% of the mitochondrial sites surveyed. The orrm5 mutant also exhibits a reduced splicing efficiency of the first nad5 intron and slower growth and delayed flowering time. ORRM5 contains an RNA recognition motif (RRM) and a glycine-rich domain at the C terminus. The RRM provides the editing activity of ORRM5 and is able to complement the splicing but not the morphological defects
Beschreibung:Date Completed 29.11.2017
Date Revised 02.12.2018
published: Print
Citation Status MEDLINE
ISSN:1460-2431
DOI:10.1093/jxb/erx139