Regulation of the Wound‐Induced Myrosinase‐Associated Protein Transcript in <i>Brassica Napus</i> Plants

Taipalensuu, Jan; Andréasson, Erik; Eriksson, Susanna; Rask, Lars

doi:10.1111/j.1432-1033.1997.00963.x

Cited by 47 publications

(41 citation statements)

References 55 publications

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“…However, two myrosinase-like genes (BGL1, At1g52400 and At5g28510) were strongly up-regulated during K 1 starvation (average fold change of 8.6 and 7.6, respectively) and down-regulated upon K 1 resupply. Furthermore, several myrosinase-binding protein, homologs of which are induced by wounding and exogenous JA treatment in Brassica napus (Taipalensuu et al, 1997), showed the same expression profile.…”

Section: Glucosinolate Synthesis and Degradationmentioning

confidence: 75%

The Potassium-Dependent Transcriptome of Arabidopsis Reveals a Prominent Role of Jasmonic Acid in Nutrient Signaling

2004

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Full genome microarrays were used to assess transcriptional responses of Arabidopsis seedlings to changing external supply of the essential macronutrient potassium (K+). Rank product statistics and iterative group analysis were employed to identify differentially regulated genes and statistically significant coregulated sets of functionally related genes. The most prominent response was found for genes linked to the phytohormone jasmonic acid (JA). Transcript levels for the JA biosynthetic enzymes lipoxygenase, allene oxide synthase, and allene oxide cyclase were strongly increased during K+ starvation and quickly decreased after K+ resupply. A large number of well-known JA responsive genes showed the same expression profile, including genes involved in storage of amino acids (VSP), glucosinolate production (CYP79), polyamine biosynthesis (ADC2), and defense (PDF1.2). Our findings highlight a novel role of JA in nutrient signaling and stress management through a variety of physiological processes such as nutrient storage, recycling, and reallocation. Other highly significant K+-responsive genes discovered in our study encoded cell wall proteins (e.g. extensins and arabinogalactans) and ion transporters (e.g. the high-affinity K+ transporter HAK5 and the nitrate transporter NRT2.1) as well as proteins with a putative role in Ca2+ signaling (e.g. calmodulins). On the basis of our results, we propose candidate genes involved in K+ perception and signaling as well as a network of molecular processes underlying plant adaptation to K+ deficiency.

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Section: Glucosinolate Synthesis and Degradationmentioning

confidence: 75%

The Potassium-Dependent Transcriptome of Arabidopsis Reveals a Prominent Role of Jasmonic Acid in Nutrient Signaling

2004

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“…However, the antagonising effect of SA on the wound-mediated and ABA-mediated increase in the amount of MBP transcript is in accordance with the effect of SA on pin2 expression (Pena-Cortes et al, 1993). Moreover, as for the wound-inducible protease-inhibitor proteins in tomato (Doares et al, 1995) and the wound-inducible MAP in B. nupus (Taipalensuu et al, 1997a), an SA-sensitive step after JA has been identified in the signal-transduction pathway regulating the wound-inducible MBP. However, the antagonising effect of SA on JA induction of MBP was much more pronounced as compared with the effect on the JA-mediated MAP induction, which might indicate the presence of at least partially different signaltransduction pathways.…”

Section: Discussionmentioning

confidence: 99%

“…The subcellular location of MAP has not been determined. However, the seed-MAP and the inducible-MAP transcripts seem to encode putative cleavable signal peptides (Taipalensuu et al, , 1997a, and MAP is a glycosylated protein that has been purified from a protein-body-enriched fraction (Falk et al, 1995a;Taipalensuu et al 1996), indicating that MAP might be targetted to the same compartment as myrosinases and MBP. Although it has not been demonstrated conclusively whether or not MAP transcripts are expressed in myrosin cells, from in situ hybridisations it is clear that the amount of MAP transcripts increases in most cells following MeJA treatment (Taipalensuu et al, 1997a).…”

Section: Discussionmentioning

confidence: 99%

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The Myrosinase‐Binding Protein from Brassica Napus Seeds Possesses lectin Activity and has a Highly Similar Vegetatively Expressed Wound‐Inducible Counterpart

Taipalensuu

Eriksson

Rask

1997

European Journal of Biochemistry

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This communication demonstrates that proteins in the family of myrosinase-binding proteins (MBP) present in seeds of Brassicu napus possess lectin activity, binding most efficiently to p-aminophenyl a-D-mannopyranoside-agarose, and to some extent to N-acetylglucosamine-agarose. A cDNA encoding a vegetatively expressed, wound-inducible counterpart to these seed MBP was isolated and characterised. Upon wounding, this MBP transcript accumulated in old and young leaves, and was systemically expressed in the young plant. Additionally, the wound-induced MBP transcript increased in abundance after treating the young plants with methyl jasmonate (MeJA), jasmonic acid (JA) or abscisic acid (ABA), and to some extent in response to the ethylene precursor 1 -aminocyclopropane-1-carboxylic acid. Expression induced by wounding, ABA or JA was antagonised by simultaneous feeding of the plants with salicylic acid. MBP polypeptides accumulated in MeJA-treated plants. The myrosinases redistributed from the soluble fraction into the insoluble fraction of a tissue extract after induction. The most abundant MBP (94 kDa) partitioned in the insoluble fraction, while two larger MBP (103 kDa and 108 kDa) were present only in the soluble fraction of extracts obtained from the control or MeJA-treated plant tissues.

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“…The enzymes that catalyze the core reactions of glucosinolate biosynthesis have been identified (Wittstock and Halkier, 2002); however, a number of glucosinolates are further modified by additions of other substituents that include sinapoyl and benzoyl groups (Linscheid et al, 1980;Reichelt et al, 2002;Brown et al, 2003). This acylation may have an impact on glucosinolate turnover and plant-herbivore interactions because they are not readily degradable targets for myrosinases (Taipalensuu et al, 1997). The presence of benzoylated glucosinolates in Arabidopsis has already been demonstrated, and sinapoylated glucosinolates have been detected in Arabidopsis seed extracts (Graser et al, 2001;Reichelt et al, 2002).…”

Section: Candidate Reactions For Scpl Acyltransferases Can Be Found Tmentioning

confidence: 99%

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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Regulation of the Wound‐Induced Myrosinase‐Associated Protein Transcript in Brassica Napus Plants

Cited by 47 publications

References 55 publications

The Potassium-Dependent Transcriptome of Arabidopsis Reveals a Prominent Role of Jasmonic Acid in Nutrient Signaling

The Potassium-Dependent Transcriptome of Arabidopsis Reveals a Prominent Role of Jasmonic Acid in Nutrient Signaling

The Myrosinase‐Binding Protein from Brassica Napus Seeds Possesses lectin Activity and has a Highly Similar Vegetatively Expressed Wound‐Inducible Counterpart

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

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