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This communication demonstrates that proteins in the family of myrosinase-binding proteins (MBP) present in seeds of Brassica napus possess lectin activity, binding most efficiently to p-aminophenyl α-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. [ABSTRACT FROM AUTHOR]

Two slightly differing cDNA clones corresponding to the wound-inducible form of a previously characterized seed myrosinase-associated protein (MyAP) have been isolated from Brassica napus L. The transcripts corresponding to the induced MyAP (iMyAP) were found to be developmentally regulated in various vegetative organs. Both young and old leaves exhibited wound-inducible iMyAP expression. Furthermore, in the young plant, wounding resulted in a systemic increase in leaves located both acropetally and basipetally to the wounded leaf. Also, the iMyAP transcripts were induced by methyl jasmonate, jasmonic acid and abscisic acid. The different inductions could be antagonized by salicylic acid. A general responsiveness in methyl-jasmonate-treated leaves was demonstrated by in situ hybridization. No effect on the amount of iMyAP transcript was detected after feeding the plants with the ethylene precursor 1aminocyclopropane-1-carboxylic acid. The similarity between MyAP and a lipase from Arabidopsis thaliana indicated a possible function in liberating acylated glucosinolates from their acyl group, thereby making them available for hydrolysis by the myrosinase enzymes. We also report on a reduction in the amount of myrosinase transcripts derived from the vegetatively expressed MB-gene family after treatment with exogenously applied salicylic acid or abscisic acid. [ABSTRACT FROM AUTHOR]

Several non-myrosinase proteins have been found in association with some of the myrosinases extracted from rape (Brassica napus) seed. Most of these proteins seemed to belong to a large family of proteins ranging in size over approximately 30-110 kDa, namely the myrosinase-binding protein (MBP) family. Potentially all of these MBPs might be derived from a single large precursor, encoded by a 3.3-kb transcript. This transcript coded for a 99-kDa glycine-rich protein with a highly repetitive structure. The mature 50-kDa and 52-kDa MBP amino-terminal was located 255 amino acids from the putative initiation methionine. Also, a more divergently related transcript, the protein product of which was unknown, has been cloned. However, the largest open reading frame suggested a proline-rich protein. While this transcript seemed to be expressed predominantly in seeds, the MBP transcripts were expressed in several tissues and also exhibited a responsiveness to wounding and methyl jasmonate. Both proteins exhibited significant similarities to lectins from Artocarpus integer arid from Maclura pomifera. [ABSTRACT FROM AUTHOR]