AtGRP5, a vacuole-located glycine-rich protein involved in cell elongation

Mangeon, Amanda; Magioli, Cláudia; Menezes-Salgueiro, Adriana Dias; Cardeal, Vanessa; Oliveira, Cristina de; Galvão, Vinícius Costa; Margis, Rogério; Engler, Gilbert; Sachetto-Martins, Gilberto

doi:10.1007/s00425-009-0940-4

Cited by 41 publications

(40 citation statements)

References 54 publications

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“…To confirm the subcellular localization of Dc AA5GT and Dg AA7GT, green fluorescent protein (GFP) fusion constructs containing either the full-length or the predicted transit peptide sequences of Dc AA5GT and Dg AA7GT driven by cauliflower mosaic virus (CaMV) 35S promoter were introduced into onion epidermal cells by microprojectile bombardment. We observed a close correspondence in the distribution pattern for Dc AA5GT-transit-peptide:GFP ( Figure 4A), Dg AA7GT-transitpeptide:GFP ( Figure 4B), and full-length-Dg AA7GT:GFP ( Figure 4D) with that of a Gly-rich protein of Arabidopsis (GRP5) that is normally located in the vacuoles ( Figure 4G) (Mangeon et al, 2009). The full-length-Dc AA5GT:GFP did not show strict localization of fluorescent signals to the vacuole but also had some signals in the cytosol ( Figure 4C).…”

Section: Subcellular Localization Of DC Aa5gt and Dg Aa7gt And Expresmentioning

confidence: 89%

A Novel Glucosylation Reaction on Anthocyanins Catalyzed by Acyl-Glucose–Dependent Glucosyltransferase in the Petals of Carnation and Delphinium

et al. 2010

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Glucosylation of anthocyanin in carnations (Dianthus caryophyllus) and delphiniums (Delphinium grandiflorum) involves novel sugar donors, aromatic acyl-glucoses, in a reaction catalyzed by the enzymes acyl-glucose-dependent anthocyanin 5 (7)-O-glucosyltransferase (AA5GT and AA7GT). The AA5GT enzyme was purified from carnation petals, and cDNAs encoding carnation Dc AA5GT and the delphinium homolog Dg AA7GT were isolated. Recombinant Dc AA5GT and Dg AA7GT proteins showed AA5GT and AA7GT activities in vitro. Although expression of Dc AA5GT in developing carnation petals was highest at early stages, AA5GT activity and anthocyanin accumulation continued to increase during later stages. Neither Dc AA5GT expression nor AA5GT activity was observed in the petals of mutant carnations; these petals accumulated anthocyanin lacking the glucosyl moiety at the 5 position. Transient expression of Dc AA5GT in petal cells of mutant carnations is expected to result in the transfer of a glucose moiety to the 5 position of anthocyanin. The amino acid sequences of Dc AA5GT and Dg AA7GT showed high similarity to glycoside hydrolase family 1 proteins, which typically act as b-glycosidases. A phylogenetic analysis of the amino acid sequences suggested that other plant species are likely to have similar acylglucose-dependent glucosyltransferases.

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Section: Subcellular Localization Of DC Aa5gt and Dg Aa7gt And Expresmentioning

confidence: 89%

A Novel Glucosylation Reaction on Anthocyanins Catalyzed by Acyl-Glucose–Dependent Glucosyltransferase in the Petals of Carnation and Delphinium

et al. 2010

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“…They were proposed to function in cell elongation, plant defense, plant stress responses, flowering, and development, etc. (Fusaro et al, 2007;Fu et al, 2007;Kim et al, 2007;Streitner et al, 2008;Mangeon et al, 2009), likely due to the variation of their domain arrangements. Despite of all the efforts in characterizing the functions of plant GRPs, little is known about the function of the GR domain in these GRPs.…”

Section: Discussionmentioning

confidence: 99%

RNA Recognition Motif-Containing Protein ORRM4 Broadly Affects Mitochondrial RNA Editing and Impacts Plant Development and Flowering

et al. 2015

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Plant RNA editosomes modify cytidines (C) to uridines (U) at specific sites in plastid and mitochondrial transcripts. Members of the RNA-editing factor interacting protein (RIP) family and Organelle RNA Recognition Motif-containing (ORRM) family are essential components of the Arabidopsis (Arabidopsis thaliana) editosome. ORRM2 and ORRM3 have been recently identified as minor mitochondrial editing factors whose silencing reduces editing efficiency at ;6% of the mitochondrial C targets. Here we report the identification of ORRM4 (for organelle RRM protein 4) as a novel, major mitochondrial editing factor that controls ;44% of the mitochondrial editing sites. C-to-U conversion is reduced, but not eliminated completely, at the affected sites. The orrm4 mutant exhibits slower growth and delayed flowering time. ORRM4 affects editing in a site-specific way, though orrm4 mutation affects editing of the entire transcript of certain genes. ORRM4 contains an RRM domain at the N terminus and a Gly-rich domain at the C terminus. The RRM domain provides the editing activity of ORRM4, whereas the Gly-rich domain is required for its interaction with ORRM3 and with itself. The presence of ORRM4 in the editosome is further supported by its interaction with RIP1 in a bimolecular fluorescence complementation assay. The identification of ORRM4 as a major mitochondrial editing factor further expands our knowledge of the composition of the RNA editosome and reveals that adequate mitochondrial editing is necessary for normal plant development.

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“…In the cells, the transit peptides of SCPL2, AA7BG-GT1, and AA7BG-GT2:GFP exhibited a similar pattern of fluorescence to a Gly-rich protein of Arabidopsis (GRP5) that is normally located in the vacuoles (see Supplemental Figure 6 online) (Mangeon et al, 2009). …”

Section: Subcellular Localization Of Scpl2 Aa7bg-gt1 and Aa7bg-gt2 mentioning

confidence: 99%

p-Hydroxybenzoyl-Glucose Is a Zwitter Donor for the Biosynthesis of 7-Polyacylated Anthocyanin in Delphinium

et al. 2013

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ORCID IDs: 0000-0002-3002-368X (Y.O.); 0000-0001-7474-9493 (N.S.).The blue color of delphinium (Delphinium grandiflorum) flowers is produced by two 7-polyacylated anthocyanins, violdelphin and cyanodelphin. Violdelphin is derived from the chromophore delphinidin that has been modified at the 7-position by Glc and p-hydroxybenzoic acid (pHBA) molecules. Modification of violdelphin by linear conjugation of Glc and pHBA molecules to a Glc moiety at the 7-position produces cyanodelphin. We recently showed that anthocyanin 7-O-glucosylation in delphinium is catalyzed by the acyl-Glc-dependent anthocyanin glucosyltransferase (AAGT). Here, we sought to answer the question of which enzyme activities are necessary for catalyzing the transfer of Glc and pHBA moieties to 7-glucosylated anthocyanin. We found that these transfers were catalyzed by enzymes that use p-hydroxybenzoyl-Glc (pHBG) as a bifunctional acyl and glucosyl donor. In addition, we determined that violdelphin is synthesized via step-by-step enzymatic reactions catalyzed by two enzymes that use pHBG as an acyl or glucosyl donor. We also isolated a cDNA encoding a protein that has the potential for p-hydroxybenzoylation activity and two AAGT cDNAs that encode a protein capable of adding Glc to delphinidin 3-Orutinoside-7-O-(6-O-[ p-hydroxybenzoyl]-glucoside) to form violdelphin.

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AtGRP5, a vacuole-located glycine-rich protein involved in cell elongation

Cited by 41 publications

References 54 publications

A Novel Glucosylation Reaction on Anthocyanins Catalyzed by Acyl-Glucose–Dependent Glucosyltransferase in the Petals of Carnation and Delphinium

A Novel Glucosylation Reaction on Anthocyanins Catalyzed by Acyl-Glucose–Dependent Glucosyltransferase in the Petals of Carnation and Delphinium

RNA Recognition Motif-Containing Protein ORRM4 Broadly Affects Mitochondrial RNA Editing and Impacts Plant Development and Flowering

p-Hydroxybenzoyl-Glucose Is a Zwitter Donor for the Biosynthesis of 7-Polyacylated Anthocyanin in Delphinium

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