DAG, a gene required for chloroplast differentiation and palisade development in Antirrhinum majus.

Chatterjee, Manash; S, Sparvoli; Edmunds, C; Garosi, P; Findlay, Kim; Martin, Cathie

doi:10.1002/j.1460-2075.1996.tb00794.x

Cited by 131 publications

(121 citation statements)

References 54 publications

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“…The MS data indicated that the protein encoded by At3g15000 was the top candidate RARE1-interacting protein present in the immunoprepitate, because it had the largest number of matches of MS/MS spectra other than RARE1 (SI Appendix, Table S1). The gene encodes a member of the differentiation and greening (DAG) family; mutants in members of this gene family exhibit chloroplast biogenesis defects (32,33). Yeast two-hybrid analysis confirmed the interaction between RARE1 and the protein encoded by At3g15000, which was, therefore, named RIP1 (SI Appendix, Fig.…”

Section: Resultsmentioning

confidence: 99%

RIP1, a member of an Arabidopsis protein family, interacts with the protein RARE1 and broadly affects RNA editing

Bentolila¹,

Heller²,

Sun³

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

214

266

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Transcripts of plant organelle genes are modified by cytidine-touridine (C-to-U) RNA editing, often changing the encoded amino acid predicted from the DNA sequence. Members of the PLS subclass of the pentatricopeptide repeat (PPR) motif-containing family are site-specific recognition factors for either chloroplast or mitochondrial C targets of editing. However, other than PPR proteins and the cis-elements on the organelle transcripts, no other components of the editing machinery in either organelle have previously been identified. The Arabidopsis chloroplast PPR protein Required for AccD RNA Editing 1 (RARE1) specifies editing of a C in the accD transcript. RARE1 was detected in a complex of >200 kDa. We immunoprecipitated epitope-tagged RARE1, and tandem MS/MS analysis identified a protein of unknown function lacking PPR motifs; we named it RNA-editing factor interacting protein 1 (RIP1). Yeast two-hybrid analysis confirmed RIP1 interaction with RARE1, and RIP1-GFP fusions were found in both chloroplasts and mitochondria. Editing assays for all 34 known Arabidopsis chloroplast targets in a rip1 mutant revealed altered efficiency of 14 editing events. In mitochondria, 266 editing events were found to have reduced efficiency, with major loss of editing at 108 C targets. Virusinduced gene silencing of RIP1 confirmed the altered editing efficiency. Transient introduction of a WT RIP1 allele into rip1 improved the defective RNA editing. The presence of RIP1 in a protein complex along with chloroplast editing factor RARE1 indicates that RIP1 is an important component of the RNA editing apparatus that acts on many chloroplast and mitochondrial C targets.nucleoid | RNA editosome | dual targeting P osttranscriptional C-to-U RNA editing occurs in plastid and plant mitochondrial transcripts. In a typical vascular plant, ∼30 C targets in chloroplasts and over 500 C targets in mitochondria are targeted for editing (1, 2). The majority of the editing events results in encoding of a different amino acid than the one predicted from the genomic sequence. The editing-encoded amino acid is usually more conserved relative to residues present in homologous proteins in other organisms than the genomically encoded amino acid. Because there is presently no known case in which useful genetic variation results from partial editing of a transcript population, the current concept is that editing is a correction mechanism for thymidine-to-cytidine (T-to-C) mutations that have arisen in plant organelle genomes (1,3,4).Little is known about the molecular apparatus that is responsible for recognizing the correct C target for editing and converting it to U, although plant mitochondrial RNA editing was discovered over 20 y ago (5-7). cis-Elements for recognition of editing sites have been identified proximal and 5′ to the nucleotide to be modified (8-10). As few as 22 nt in sequence surrounding the C target is sufficient to specify RNA editing (9). In 2005, a pentatricopeptide repeat (PPR) motif-containing protein termed CRR4 was discovered to ...

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Section: Resultsmentioning

confidence: 99%

RIP1, a member of an Arabidopsis protein family, interacts with the protein RARE1 and broadly affects RNA editing

Bentolila¹,

Heller²,

Sun³

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

214

266

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“…Identification of this type of communication has come from an examination of a handful of nuclear gene-induced pigment mutants whose white leaf tissues have abnormal plastids and cells, and altered palisade and/or spongy mesophyll cell layer organizations. These include dag of Antirrhinum majus (Chatterjee et al, 1996), dcl of tomato (Keddie et al, 1996), and several Arabidopsis mutants, including cla1 (Mandel et al, 1996;Estévez et al, 2000), cue1 (Li et al, 1995;Streatfield et al, 1999), and pac (Reiter et al, 1994;Meurer et al, 1998). Because the products of the genes defined by these mutations reside in the plastid, it has been argued that these proteins are not independently required for plastid development and cell differentiation (and consequently for proper leaf morphogenesis), but that the effects on mesophyll cell differentiation are a consequence of incomplete chloroplast differentiation.…”

Section: Plastid-to-nucleus Communication Regulates Leaf Developmentmentioning

confidence: 99%

The Arabidopsis immutans Mutation Affects Plastid Differentiation and the Morphogenesis of White and Green Sectors in Variegated Plants

et al. 2001

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The immutans (im) variegation mutant of Arabidopsis has green and white leaf sectors due to the action of a nuclear recessive gene, IMMUTANS (IM). This gene encodes the IM protein, which is a chloroplast homolog of the mitochondrial alternative oxidase. Because the white sectors of im accumulate the noncolored carotenoid, phytoene, IM likely serves as a redox component in phytoene desaturation. In this paper, we show that IM has a global impact on plant growth and development and is required for the differentiation of multiple plastid types, including chloroplasts, amyloplasts, and etioplasts. IM promoter activity and IM mRNAs are also expressed ubiquitously in Arabidopsis. IM transcript levels correlate with carotenoid accumulation in some, but not all, tissues. This suggests that IM function is not limited to carotenogenesis. Leaf anatomy is radically altered in the green and white sectors of im: Mesophyll cell sizes are dramatically enlarged in the green sectors and palisade cells fail to expand in the white sectors. The green im sectors also have significantly higher than normal rates of O 2 evolution and elevated chlorophyll a/b ratios, typical of those found in "sun" leaves. We conclude that the changes in structure and photosynthetic function of the green leaf sectors are part of an adaptive mechanism that attempts to compensate for a lack of photosynthesis in the white leaf sectors, while maximizing the ability of the plant to avoid photodamage.Variegation mutants provide an excellent system to explore the nature of communication between the nucleus-cytoplasm, chloroplast, and mitochondrial genetic compartments (for review, see Leó n et al., 1998; Rodermel, 2001). The leaves of these mutants have green and white (or yellow) sectors that arise as a consequence of mutations in nuclear or organellar genes (Tilney-Bassett, 1975). Whereas the green sectors contain cells with morphologically normal chloroplasts, cells in the white sectors contain plastids that lack pigments and normal lamellar structures. One common mechanism of variegation involves the induction of defective mitochondria or chloroplasts by mutations in nuclear genes for organelle proteins. This is sometimes due to transposable element activity, in which case the green and white cells have different genotypes. In other cases, the two types of cells have the same (mutant) genotype, indicating that the gene defined by the mutation codes for a product that is required for organelle biogenesis in some, but not all, cells of the mutant.Despite the large number of mutant screens that have been conducted in Arabidopsis, surprisingly few nuclear "variegation" loci have been reported. These include cab underexpressed (cue1), chloroplast mutator (chm), differential development of vascularassociated cells (dov), immutans (im), pale cress (pac), var1, and var2 (e.g.

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“…Up to 15 transgenic tobacco plants transformed with each construct under the control of the double CaMV 35S promoter were examined for the levels of the bZIP transcripts in leaves. Leaves from selected plants expressing high levels of each transgene were also examined for transcript levels of histone genes (H4) (Forbert et al, 1994) and members of the tobacco CAB gene family (Chatterjee et al, 1996) and the small subunit gene of Rubisco (RBCS), by probing RNA gel blots. Loading was quantified by probing with the rDNA from pea to identify ribosomal RNA and with a UBIQUITIN cDNA clone from Antirrhinum.…”

Section: Bzip910 and Bzip911 Can Alter Histone And Cab Transcript Levmentioning

confidence: 99%

“…Three independent transformants expressing bZIP910 with its 5Ј leader (910L) and without its 5Ј leader (910S), three independent transformants expressing bZIP911 with its 5Ј leader (911L) and one expressing bZIP911 without its 5Ј leader (911S) were compared to plants expressing bZIP910 and bZIP911 in antisense orientation (AS910 and AS911, respectively) and the average of two control plants transformed with vector alone (C). RNA gel blots were probed with genes encoding histone H4 (from Antirrhinum majus; a gift from John Doonan, Forbert et al, 1994), CAB (from tobacco; Chatterjee et al, 1996) and ubiquitin (from Antirrhinum majus). Transcript levels were quantified by phosphor imager and values were corrected for small variations in loading by standardization to the ubiquitin values.…”

Section: Bzip910 and Bzip911 Can Alter Histone And Cab Transcript Levmentioning

confidence: 99%

Two bZIP proteins from Antirrhinum flowers preferentially bind a hybrid C‐box/G‐box motif and help to define a new sub‐family of bZIP transcription factors

et al. 1998

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SummaryTwo genes encoding bZIP proteins are expressed in flowers of Antirrhinum majus, predominantly in vascular tissues, carpels and anthers. The sequences of cDNA clones encoding these proteins show them to belong to a distinct subfamily of bZIP proteins which also includes LIP19 from rice and MLIPI5 and OBF1 from maize. The sub-family is characterized by the inclusion of very small proteins consisting of essentially a basic domain and a long leucine zipper. Members also have a conserved upstream open reading frame (uORF) in their 5Ј leader sequences, implying a common mode of post-transcriptional control. In vitro, the Antirrhinum bZIP proteins preferentially bind to a novel hybrid C-box/G-box motif which is found in the promoters of some plant histone genes and of some nuclear-encoded genes with plastidial protein products. Expression of the bZIP proteins in transgenic tobacco under control of the CaMV 35S promoter supports the view that they can regulate expression of genes which contain the preferred target motif within their regulatory sequences, although both enhancement and repression of transcript levels of target genes were observed, indicating that the bZIP proteins probably interact with other factors to modulate transcription in different ways, as has been observed for the small MAF family of bZIP proteins in vertebrates.

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DAG, a gene required for chloroplast differentiation and palisade development in Antirrhinum majus.

Cited by 131 publications

References 54 publications

RIP1, a member of an Arabidopsis protein family, interacts with the protein RARE1 and broadly affects RNA editing

RIP1, a member of an Arabidopsis protein family, interacts with the protein RARE1 and broadly affects RNA editing

The Arabidopsis immutans Mutation Affects Plastid Differentiation and the Morphogenesis of White and Green Sectors in Variegated Plants

Two bZIP proteins from Antirrhinum flowers preferentially bind a hybrid C‐box/G‐box motif and help to define a new sub‐family of bZIP transcription factors

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