Characterisation of the genes for ribosomal RNA in flax

Goldsbrough, Peter B.; Cullis, Christopher A.

doi:10.1093/nar/9.6.1301

Cited by 136 publications

(69 citation statements)

References 18 publications

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“…RNA was extracted from tissues (Goldsbrough and Cullis, 1981), electrophoretically separated, transferred to Hybond N ϩ membrane (Amersham), and hybridized with radiolabeled probes prepared from genomic clones according to standard protocols. The genomic and cDNA clones were sequenced on a Pharmacia (Uppsala, Sweden) ALFexpress automated DNA sequencer with the use of standard primers.…”

Section: Analysis Of Nucleic Acidsmentioning

confidence: 99%

Cloning of the SNG1 Gene of Arabidopsis Reveals a Role for a Serine Carboxypeptidase-like Protein as an Acyltransferase in Secondary Metabolism

et al. 2000

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Serine carboxypeptidases contain a conserved catalytic triad of serine, histidine, and aspartic acid active-site residues. These enzymes cleave the peptide bond between the penultimate and C-terminal amino acid residues of their protein or peptide substrates. The Arabidopsis Genome Initiative has revealed that the Arabidopsis genome encodes numerous proteins with homology to serine carboxypeptidases. Although many of these proteins may be involved in protein turnover or processing, the role of virtually all of these serine carboxypeptidase-like (SCPL) proteins in plant metabolism is unknown. We previously identified an Arabidopsis mutant, sng1 (sinapoylglucose accumulator 1), that is defective in synthesis of sinapoylmalate, one of the major phenylpropanoid secondary metabolites accumulated by Arabidopsis and some other members of the Brassicaceae. We have cloned the gene that is defective in sng1 and have found that it encodes a SCPL protein. Expression of SNG1 in Escherichia coli demonstrates that it encodes sinapoylglucose:malate sinapoyltransferase, an enzyme that catalyzes a transesterification instead of functioning like a hydrolase, as do the other carboxypeptidases. This finding suggests that SCPL proteins have acquired novel functions in plant metabolism and provides an insight into the evolution of secondary metabolic pathways in plants. INTRODUCTIONPlants produce thousands of unique molecules that are collectively referred to as secondary metabolites. Even within the angiosperms, many of these compounds are unique to specific taxa, indicating that the pathways that produce them may have evolved within the last 100,000 years. A central question in the study of plant secondary metabolism concerns how the catalytic diversity of plant secondary metabolism has arisen. What classes of genes and proteins have been co-opted, presumably from their ancestral roles in primary metabolism, to serve as catalysts in the synthesis of secondary metabolites?In Arabidopsis, the phenylpropanoid pathway leads to the production of sinapic acid esters, a group of fluorescent UVprotective secondary metabolites derived from phenylalanine (Figure 1). These compounds are dispensable under laboratory conditions and thus provide targets for the genetic dissection of phenylpropanoid metabolism. The analysis of these compounds is facilitated by their blue fluorescence under UV light both in vivo and after thin-layer chromatography (TLC) (Chapple et al., 1992;Ruegger et al., 1999). Arabidopsis and some other members of the Brassicaceae accumulate three major sinapic acid esters. In the biosynthetic pathway leading to these compounds, sinapoylglucose is the immediate precursor of sinapoylcholine and sinapoylmalate, which accumulate in seeds and leaves, respectively. 1-O -Sinapoylglucose is a ␤ -acetal ester with a high free energy of hydrolysis (Mock and Strack, 1993); it provides the necessary free energy for the transacylation reaction catalyzed by sinapoylglucose:malate sinapoyltransferase (SMT; EC 2.3.1.92) (Strack, 1982), which ...

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Section: Analysis Of Nucleic Acidsmentioning

confidence: 99%

Cloning of the SNG1 Gene of Arabidopsis Reveals a Role for a Serine Carboxypeptidase-like Protein as an Acyltransferase in Secondary Metabolism

et al. 2000

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“…The gene-specific probe DCACS2-3Ј corresponds to bp 429 to 709. To demonstrate equal loading of RNA samples, membranes were reprobed with rRNA (Goldsbrough and Cullis, 1981).…”

Section: Rna Extraction and Gel-blot Analysismentioning

confidence: 99%

Differential Expression of Three Members of the 1-Aminocyclopropane-1-Carboxylate Synthase Gene Family in Carnation1

Jones¹,

Woodson

1999

Plant Physiology

141

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We investigated the expression patterns of three 1-aminocyclopropane-1-carboxylate (ACC) synthase genes in carnation (Dianthus caryophyllus cv White Sim) under conditions previously shown to induce ethylene biosynthesis. These included treatment of flowers with 2,4-dichlorophenoxyacetic acid, ethylene, LiCl, cycloheximide, and natural and pollination-induced flower senescence. Accumulation of ACC synthase transcripts in leaves following mechanical wounding and treatment with 2,4-dichlorophenoxyacetic acid or LiCl was also determined by RNA gel-blot analysis. As in other species, the carnation ACC synthase genes were found to be differentially regulated in a tissue-specific manner. DCACS2 and DCACS3 were preferentially expressed in styles, whereas DCACS1 mRNA was most abundant in petals. Cycloheximide did not induce increased accumulation of ACC synthase transcripts in carnation flowers, whereas the expression of ACC synthase was up-regulated by auxin, ethylene, LiCl, pollination, and senescence in a floralorgan-specific manner. Expression of the three ACC synthases identified in carnation did not correspond to elevated ethylene biosynthesis from wounded or auxin-treated leaves, and there are likely additional members of the carnation ACC synthase gene family responsible for ACC synthase expression in vegetative tissues.

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“…After hybridization the blots were washed under high-stringency conditions (2ϫ SSC, 0.1% [w/v] SDS, room temperature; 0.5ϫ SSC, 0.1% [w/v] SDS, 55°C; 0.1ϫ SSC, 0.1% [w/v] SDS, 68°C). Equal loading of RNA was confirmed by staining with ethidium bromide, stripping the blots, and reprobing with a 32 P-labeled 25S ribosomal cDNA probe from Linum usitatissium (Goldsbrough and Cullis, 1981) using the same hybridization and washing conditions described above.…”

Section: Northern Analysismentioning

confidence: 99%

Functional Characterization and Expression Analysis of the Amino Acid Permease RcAAP3 from Castor Bean1

Neelam¹,

Marvier

Hall

et al. 1999

Plant Physiology

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A polymerase chain reaction-based library screening procedure was used to isolate RcAAP3, an amino acid permease cDNA from castor bean (Ricinus communis). RcAAP3 is 1.7 kb in length, with an open reading frame that encodes a protein with a calculated molecular mass of 51 kD. Hydropathy analysis indicates that the RcAAP3 protein is highly hydrophobic in nature with nine to 11 putative transmembrane domains. RcAAP3-mediated uptake of citrulline in a yeast transport mutant showed saturable kinetics with a K m of 0.4 mM. Transport was higher at acidic pH and was inhibited by the protonophore carbonylcyanide-m-chlorophenylhydrazone, suggesting a proton-coupled transport mechanism. Citrulline uptake was strongly inhibited (72%) by the permeable sulfydryl reagent N-ethylmaleimide, but showed lower sensitivity (30% inhibition) to the nonpermeable reagent p-chloromercuribenzenesulfonic acid. Diethylpyrocarbonate, a histidine modifier, inhibited citrulline uptake by 80%. A range of amino acids inhibited citrulline uptake, suggesting that RcAAP3 may be a broad substrate permease that can transport neutral and basic amino acids with a lower affinity for acidic amino acids. Northern analysis indicated that RcAAP3 is widely expressed in source and sink tissues of castor bean, and that the pattern of expression is distinct from RcAAP1 and RcAAP2.

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Characterisation of the genes for ribosomal RNA in flax

Cited by 136 publications

References 18 publications

Cloning of the SNG1 Gene of Arabidopsis Reveals a Role for a Serine Carboxypeptidase-like Protein as an Acyltransferase in Secondary Metabolism

Cloning of the SNG1 Gene of Arabidopsis Reveals a Role for a Serine Carboxypeptidase-like Protein as an Acyltransferase in Secondary Metabolism

Differential Expression of Three Members of the 1-Aminocyclopropane-1-Carboxylate Synthase Gene Family in Carnation1

Functional Characterization and Expression Analysis of the Amino Acid Permease RcAAP3 from Castor Bean1

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