RIP1, a member of an Arabidopsis protein family, interacts with the protein RARE1 and broadly affects RNA editing.
about
Complex RNA metabolism in the chloroplast: an update on the psbB operonThe Pet309 pentatricopeptide repeat motifs mediate efficient binding to the mitochondrial COX1 transcript in yeast.RNA Editing and Its Molecular Mechanism in Plant OrganellesAbundant RNA editing sites of chloroplast protein-coding genes in Ginkgo biloba and an evolutionary pattern analysis.Comprehensive High-Resolution Analysis of the Role of an Arabidopsis Gene Family in RNA EditingAn RNA recognition motif-containing protein is required for plastid RNA editing in Arabidopsis and maize.The Schizosaccharomyces pombe PPR protein Ppr10 associates with a novel protein Mpa1 and acts as a mitochondrial translational activator.Functional divergence and origin of the DAG-like gene family in plants.Elucidation of the RNA recognition code for pentatricopeptide repeat proteins involved in organelle RNA editing in plants.The tomato mutation nxd1 reveals a gene necessary for neoxanthin biosynthesis and demonstrates that violaxanthin is a sufficient precursor for abscisic acid biosynthesis.MEF10 is required for RNA editing at nad2-842 in mitochondria of Arabidopsis thaliana and interacts with MORF8.Mediated plastid RNA editing in plant immunityCytidine deaminase motifs within the DYW domain of two pentatricopeptide repeat-containing proteins are required for site-specific chloroplast RNA editing.Deletions in cox2 mRNA result in loss of splicing and RNA editing and gain of novel RNA editing sites.A conserved glutamate residue in the C-terminal deaminase domain of pentatricopeptide repeat proteins is required for RNA editing activity.Two RNA recognition motif-containing proteins are plant mitochondrial editing factorsA zinc finger motif-containing protein is essential for chloroplast RNA editing.The DYW Subgroup PPR Protein MEF35 Targets RNA Editing Sites in the Mitochondrial rpl16, nad4 and cob mRNAs in Arabidopsis thaliana.Frequent chloroplast RNA editing in early-branching flowering plants: pilot studies on angiosperm-wide coexistence of editing sites and their nuclear specificity factorsReverse U-to-C editing exceeds C-to-U RNA editing in some ferns - a monilophyte-wide comparison of chloroplast and mitochondrial RNA editing suggests independent evolution of the two processes in both organelles.Functional remodeling of RNA processing in replacement chloroplasts by pathways retained from their predecessors.Distinct role of Arabidopsis mitochondrial P-type pentatricopeptide repeat protein-modulating editing protein, PPME, in nad1 RNA editingOrganelle RNA recognition motif-containing (ORRM) proteins are plastid and mitochondrial editing factors in Arabidopsis.Pentatricopeptide repeats: modular blocks for building RNA-binding proteins.Quantitative trait locus mapping identifies REME2, a PPR-DYW protein required for editing of specific C targets in Arabidopsis mitochondria.A survey of PPR proteins identifies DYW domains like those of land plant RNA editing factors in diverse eukaryotes.Identification of two pentatricopeptide repeat genes required for RNA editing and zinc binding by C-terminal cytidine deaminase-like domains.Tetrapyrrole biosynthetic enzyme protoporphyrinogen IX oxidase 1 is required for plastid RNA editingRNA processing and decay in plastids.Mitochondrial RNA editing PPR proteins can tolerate protein tags at E as well as at DYW domain termini.A Single-Target Mitochondrial RNA Editing Factor of Funaria hygrometrica Can Fully Reconstitute RNA Editing at Two Sites in Physcomitrella patens.Plants grow with a little help from their organelle friends.Functional diversity of Arabidopsis organelle-localized RNA-recognition motif-containing proteins.Functional analysis of the Arabidopsis thaliana CHLOROPLAST BIOGENESIS 19 pentatricopeptide repeat editing protein.Whole plastid transcriptomes reveal abundant RNA editing sites and differential editing status in Phalaenopsis aphrodite subsp. formosana.Function of PPR proteins in plastid gene expression.Crystal structures of the Arabidopsis thaliana organellar RNA editing factors MORF1 and MORF9.The E domains of pentatricopeptide repeat proteins from different organelles are not functionally equivalent for RNA editing.A protein with an unusually short PPR domain, MEF8, affects editing at over 60 Arabidopsis mitochondrial C targets of RNA editing.The longest mitochondrial RNA editing PPR protein MEF12 in Arabidopsis thaliana requires the full-length E domain.
P2860
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P2860
RIP1, a member of an Arabidopsis protein family, interacts with the protein RARE1 and broadly affects RNA editing.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
2012年论文
@zh
2012年论文
@zh-cn
name
RIP1, a member of an Arabidops ...... d broadly affects RNA editing.
@ast
RIP1, a member of an Arabidops ...... d broadly affects RNA editing.
@en
type
label
RIP1, a member of an Arabidops ...... d broadly affects RNA editing.
@ast
RIP1, a member of an Arabidops ...... d broadly affects RNA editing.
@en
prefLabel
RIP1, a member of an Arabidops ...... d broadly affects RNA editing.
@ast
RIP1, a member of an Arabidops ...... d broadly affects RNA editing.
@en
P2093
P2860
P356
P1476
RIP1, a member of an Arabidops ...... d broadly affects RNA editing.
@en
P2093
Arianne M Babina
Giulia Friso
Klaas J van Wijk
Stephane Bentolila
Wade P Heller
P2860
P304
P356
10.1073/PNAS.1121465109
P407
P577
2012-05-07T00:00:00Z