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

Lehfeldt, Claus; Shirley, Amber M.; Meyer, Knut Andreas; Ruegger, Max O.; Cusumano, Joanne C.; Viitanen, Paul V.; Strack, Dieter; Chapple, Clint

doi:10.2307/3871130

Cited by 94 publications

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“…One of these (At2g22960) was previously identified as a pseudogene because the ATPase-like sequences upstream of the first exon suggest that this SCPL gene lacks a promoter (Lehfeldt et al, 2000). The predicted translation products of another two (At3g56540 and At5g22960) terminate shortly after the putative catalytic Ser, and thus lack the active site Asp and His residues.…”

Section: The Arabidopsis Genome Encodes 51 Scpl Proteinsmentioning

confidence: 99%

“…The SCPL proteins of Clade IA include the known acyltransferases SMT (SCPL protein 8) and SCT (SCPL protein 19; Fig. 1A; Lehfeldt et al, 2000;Shirley et al, 2001). Several subclades of Clade IA are associated with clusters of SCPL genes that are tandemly arranged in the genome.…”

Section: Most Arabidopsis Scpl Proteins Can Be Grouped Into Two Majormentioning

confidence: 99%

“…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).…”

mentioning

confidence: 99%

“…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.…”

mentioning

confidence: 99%

“…Two enzymes in Arabidopsis (Arabidopsis thaliana) responsible for sinapate ester biosynthesis are also SCPL proteins. Sinapoylglucose:malate sinapoyltransferase (SMT) catalyzes the formation of sinapoylmalate, a UV-protectant in seedlings (Landry et al, 1995;Lehfeldt et al, 2000) and sinapoylglucose: choline sinapoyltransferase (SCT) is required for the formation of sinapoylcholine in Arabidopsis seeds (Shirley et al, 2001). …”

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confidence: 99%

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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: The Arabidopsis Genome Encodes 51 Scpl Proteinsmentioning

confidence: 99%

Section: Most Arabidopsis Scpl Proteins Can Be Grouped Into Two Majormentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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

2005

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Overexpression of a serine carboxypeptidase increases carpel number and seed production in Arabidopsis thaliana

Wen

Walker

2012

Food and Energy Security

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Seed production is an ultimate component of crop yield. Increasing seed production has long been a pursuit for crop breeders and is an indisputable measure of food safety. Advances in biotechnology can provide novel means to achieve increased seed production by genetic engineering. Overexpression of ECS1 (Extra Carpels and Seeds), a gene encoding a serine carboxypeptidase, partially suppresses the leaf phenotypes of mutant bri1‐5, a weak allele of brassinosteroid‐insensitive 1 (BRI1). Moreover, overexpression of ECS1 increases the number of carpels and seeds per fruit (silique) in Arabidopsis thaliana. Most of the ECS1‐overexpressing lines have three‐carpel siliques instead of two‐carpel siliques found in wild type, while some even have four‐carpel siliques. Wild‐type plants have an average seed number of 66.2 ± 3.6 per silique, whereas ECS1‐overexpressing lines contain 88.1 ± 4.1 seeds per silique. The total seed weight per silique increases by about 33% in ECS1‐overexpressing plants due to the increased total number of seeds. In addition, ECS1 overexpression enhances the multi‐carpel phenotypes in clavata3‐2 and causes severely fasciated stems in det2 mutants. To the best of our knowledge, it has not been previously shown that overexpressions of genes that encode serine carboxypeptidases are implicated in reproductive development or produce an increased carpel and seed numbers in any plant species.

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

Hause

Meyer

Viitanen

et al. 2002

Planta

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The serine carboxypeptidase-like protein 1- O-sinapoylglucose:malate sinapoyltransferase (SMT) catalyzes the transfer of the sinapoyl moiety of 1- O-sinapoylglucose to malate in the formation of sinapoylmalate in some members of the Brassicaceae. Rabbit polyclonal monospecific antibodies were raised against the recombinant SMT produced in Escherichia coli from the corresponding Arabidopsis thaliana (L.) Heynh. cDNA. Immunoblot analysis of protein from different Arabidopsis tissues showed that the SMT is produced in all plant organs, except in the seeds and young seedlings. The enzyme was most abundant in older seedlings as well as in rosette leaves and the flowering stem of the plant. Minor amounts were found in the cauline leaves, flower buds and siliques. Traces were detected in the root and flowers. Arabidopsis and transgenic tobacco ( Nicotiana tabacum L.) plants expressing the full-length Arabidopsis SMT containing an N-terminal signal peptide showed apparent molecular masses of the protein of 52-55 kDa. The difference of ca. 8 kDa compared to the recombinant protein produced in E. coli was shown to be due to post-translational N-glycosylation of SMT in plants. Immunofluorescent labeling of Arabidopsis leaf sections localized SMT to the central vacuoles of mesophyll and epidermal cells. Comparable leaf sections of an SMT deletion mutant showed no vacuolar immunofluorescent labeling. We conclude that Arabidopsis SMT is synthesized as a precursor protein that is targeted to the endoplasmic reticulum where the signal peptide is removed. The correct N-terminus of the recombinantly produced SMT protein lacking the signal peptide was confirmed by Edman degradation. The protein is probably glycosylated in the Golgi apparatus from where it is subsequently routed to the vacuole.

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

Cited by 94 publications

References 0 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

Overexpression of a serine carboxypeptidase increases carpel number and seed production in Arabidopsis thaliana

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

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