Immunolocalization of 1- O -sinapoylglucose:malate sinapoyltransferase in Arabidopsis thaliana

Hause, Bettina; Meyer, Knut; Viitanen, Paul V.; Chapple, Clint; Strack, Dieter

doi:10.1007/s00425-001-0716-y

Cited by 53 publications

(47 citation statements)

References 48 publications

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“…The identification of signal peptides via SignalP in 49 of the 51 SCPL proteins is consistent with experimental work showing that CPY and SMT are transported to the vacuole (Marshall, 1972;Stevens et al, 1982;Sharma and Strack, 1985;Valls et al, 1987;Hause et al, 2002). The SignalP results are also supported by the fact that the signal peptide sequence removed from the mature form of SMT (Lehfeldt et al, 2000) is accurately predicted by the algorithm.…”

Section: Arabidopsis Scpl Proteins Have Structural Features In Commonsupporting

confidence: 82%

An Expression and Bioinformatics Analysis of the Arabidopsis Serine Carboxypeptidase-Like Gene Family

2005

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The Arabidopsis (Arabidopsis thaliana) genome encodes a family of 51 proteins that are homologous to known serine carboxypeptidases. Based on their sequences, these serine carboxypeptidase-like (SCPL) proteins can be divided into several major clades. The first group consists of 21 proteins which, despite the function implied by their annotation, includes two that have been shown to function as acyltransferases in plant secondary metabolism: sinapoylglucose:malate sinapoyltransferase and sinapoylglucose:choline sinapoyltransferase. A second group comprises 25 SCPL proteins whose biochemical functions have not been clearly defined. Genes encoding representatives from both of these clades can be found in many plants, but have not yet been identified in other phyla. In contrast, the remaining SCPL proteins include five members that are similar to serine carboxypeptidases from a variety of organisms, including fungi and animals. Reverse transcription PCR results suggest that some SCPL genes are expressed in a highly tissue-specific fashion, whereas others are transcribed in a wide range of tissue types. Taken together, these data suggest that the Arabidopsis SCPL gene family encodes a diverse group of enzymes whose functions are likely to extend beyond protein degradation and processing to include activities such as the production of secondary metabolites.Serine carboxypeptidases (SCPs) are members of the a/b hydrolase family of proteins, which make use of a Ser-Asp-His catalytic triad to cleave the carboxyterminal peptide bonds of their protein or peptide substrates (Hayashi et al., 1973(Hayashi et al., , 1975Bech and Breddam, 1989;Liao and Remington, 1990;Liao et al., 1992;Ollis et al., 1992). Proteins that contain this catalytic triad and are otherwise homologous to SCPs have been found in a variety of organisms (Doi et al., 1980;Kim and Hayashi, 1983;Breddam, 1986;Baulcombe et al., 1987;Galjart et al., 1988;Bradley, 1992;Degan et al., 1994;Endrizzi et al., 1994;Wajant et al., 1994;Jones et al., 1996;Li and Steffens, 2000). Many of these serine carboxypeptidase-like (SCPL) proteins have been annotated as peptidases based only on this shared sequence similarity; however, studies have shown that some of them function not as peptidases, but as acyltransferases and lyases (Wajant et al., 1994;Lehfeldt et al., 2000;Li and Steffens, 2000;Shirley et al., 2001). For example, several SCPL proteins have been shown to catalyze the production of plant secondary metabolites involved in herbivory defense and UV protection (Wajant et al., 1994;Lehfeldt et al., 2000;Li and Steffens, 2000), including the hydroxynitrile lyase from Sorghum bicolor (SbHNL) necessary for cyanogenesis, and the acyltransferases in wild tomato (Lycopersicon pennellii) that catalyze the formation 2,3,4-isobutyryl-Glc (Wajant et al., 1994;Lehfeldt et al., 2000). Two enzymes in Arabidopsis (Arabidopsis thaliana) responsible for sinapate ester biosynthesis are also SCPL proteins. Sinapoylglucose:malate sinapoyltransferase (SMT) catalyzes the formation of s...

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Section: Arabidopsis Scpl Proteins Have Structural Features In Commonsupporting

confidence: 82%

An Expression and Bioinformatics Analysis of the Arabidopsis Serine Carboxypeptidase-Like Gene Family

2005

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“…In recent years, it has been suggested that monolignols can be glucosylated and stored as such in the vacuoles (Miao and Liu, 2010), a feature they share with some phenylpropanoid precursors (Figure 2). For example, sinapoyl glucose and sinapoyl malate are present in the vacuoles of Arabidopsis cells (Hause et al, 2002). However, the bulk of the monolignols will be exported to the cell wall for oxidation by peroxidase and/or laccase whereupon the resulting radicals cross-couple nonstereospecifically to form the lignin polymer Vanholme et al, 2012a).…”

Section: Discussionmentioning

confidence: 99%

“…In addition, phenylpropanoic acids in Arabidopsis thaliana are often derivatized to glucose esters (e.g., sinapoyl glucose). Since sinapoylglucose:malate sinapoyltransferase, catalyzing the conversion of sinapoyl glucose to sinapoyl malate, is present in the vacuole (Sharma and Strack, 1985;Hause et al, 2002), and because monolignol glucosides can be transported through the tonoplast via ATP binding cassette-like transporters (Miao and Liu, 2010), sinapoyl glucose and the monolignol glucosides are likely stored in the vacuole. A vacuolar localization of coniferin and other monolignol glucosides has been speculated (Leinhos and Savidge, 1993;Dharmawardhana et al, 1995) but has not yet been unambiguously proven (Kaneda et al, 2008).…”

Section: Introductionmentioning

confidence: 99%

Small Glycosylated Lignin Oligomers Are Stored in Arabidopsis Leaf Vacuoles

et al. 2015

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Lignin is an aromatic polymer derived from the combinatorial coupling of monolignol radicals in the cell wall. Recently, various glycosylated lignin oligomers have been revealed in Arabidopsis thaliana. Given that monolignol oxidation and monolignol radical coupling are known to occur in the apoplast, and glycosylation in the cytoplasm, it raises questions about the subcellular localization of glycosylated lignin oligomer biosynthesis and their storage. By metabolite profiling of Arabidopsis leaf vacuoles, we show that the leaf vacuole stores a large number of these small glycosylated lignin oligomers. Their structural variety and the incorporation of alternative monomers, as observed in Arabidopsis mutants with altered monolignol biosynthesis, indicate that they are all formed by combinatorial radical coupling. In contrast to the common believe that combinatorial coupling is restricted to the apoplast, we hypothesized that the aglycones of these compounds are made within the cell. To investigate this, leaf protoplast cultures were cofed with 13 C 6 -labeled coniferyl alcohol and a 13 C 4 -labeled dimer of coniferyl alcohol. Metabolite profiling of the cofed protoplasts provided strong support for the occurrence of intracellular monolignol coupling. We therefore propose a metabolic pathway involving intracellular combinatorial coupling of monolignol radicals, followed by oligomer glycosylation and vacuolar import, which shares characteristics with both lignin and lignan biosynthesis.

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“…The presence of the predicted signal peptide suggests targeting of the protein to the secretory pathway or, more likely, to the vacuole. Avenacins are known to accumulate in the vacuoles of oat root epidermal cells (Mylona et al, 2008), and the only SCPL acyltransferase that has been localized to date (the Arabidopsis 1-O-sinapoylglucose:malate sinapoyltransferase) is found in the vacuole (Hause et al, 2002).…”

Section: The Scpl1 Protein Is Posttranslationally Processed and Is LImentioning

confidence: 99%

“…However, not all SCPL proteins undergo such processing (Hause et al, 2002;Stehle et al, 2006). Comparison of the amino acid sequences of oat SCPL1 with those of characterized SCP and SCPL proteins (some of which undergo cleavage and some of which do not) reveals that SCPL1 has an extended linker region typical of SCPL proteins that are cleaved into two subunits ( Figure 7A).…”

Section: The Scpl1 Protein Is Posttranslationally Processed and Is LImentioning

confidence: 99%

A Serine Carboxypeptidase-Like Acyltransferase Is Required for Synthesis of Antimicrobial Compounds and Disease Resistance in Oats

et al. 2009

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Serine carboxypeptidase-like (SCPL) proteins have recently emerged as a new group of plant acyltransferases. These enzymes share homology with peptidases but lack protease activity and instead are able to acylate natural products. Several SCPL acyltransferases have been characterized to date from dicots, including an enzyme required for the synthesis of glucose polyesters that may contribute to insect resistance in wild tomato (Solanum pennellii) and enzymes required for the synthesis of sinapate esters associated with UV protection in Arabidopsis thaliana. In our earlier genetic analysis, we identified the Saponin-deficient 7 (Sad7) locus as being required for the synthesis of antimicrobial triterpene glycosides (avenacins) and for broad-spectrum disease resistance in diploid oat (Avena strigosa). Here, we report on the cloning of Sad7 and show that this gene encodes a functional SCPL acyltransferase, SCPL1, that is able to catalyze the synthesis of both N-methyl anthraniloyl-and benzoyl-derivatized forms of avenacin. Sad7 forms part of an operon-like gene cluster for avenacin synthesis. Oat SCPL1 (SAD7) is the founder member of a subfamily of monocot-specific SCPL proteins that includes predicted proteins from rice (Oryza sativa) and other grasses with potential roles in secondary metabolism and plant defense.

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Immunolocalization of 1- O -sinapoylglucose:malate sinapoyltransferase in Arabidopsis thaliana

Cited by 53 publications

References 48 publications

An Expression and Bioinformatics Analysis of the Arabidopsis Serine Carboxypeptidase-Like Gene Family

An Expression and Bioinformatics Analysis of the Arabidopsis Serine Carboxypeptidase-Like Gene Family

Small Glycosylated Lignin Oligomers Are Stored in Arabidopsis Leaf Vacuoles

A Serine Carboxypeptidase-Like Acyltransferase Is Required for Synthesis of Antimicrobial Compounds and Disease Resistance in Oats

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