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. 1996 Feb;110(2):483–491. doi: 10.1104/pp.110.2.483

A wound- and methyl jasmonate-inducible transcript coding for a myrosinase-associated protein with similarities to an early nodulin.

J Taipalensuu 1, A Falk 1, L Rask 1
PMCID: PMC157743  PMID: 8742330

Abstract

Myrosinase is regarded as a defense-related enzyme in the Brassicaceae and is capable of hydrolyzing glucosinolates into various compounds, some of which are toxic. Several myrosinase isoenzymes exist, and some of them have been found in association with nonmyrosinase proteins. One of these associated proteins, myrosinase-associated protein (MyAP), was purified from seeds of Brassica napus both in complexes with myrosinase and in a free form. MyAP is a glycosylated, 40-kD protein with at least one intramolecular disufide bridge. A monoclonal anti-MyAP antibody precipitated myrosinase activity from B. napus seed extracts and in these complexes both a 65- and a 70-kD myrosinase were present. The subsequent cloning and analysis revealed the existence of a gene family encoding MyAP or MyAP-related protein and that transcripts corresponding to MyAP in nonwounded plants are found predominantly in seeds. At least some members of the gene family exhibited responsiveness toward wounding and methyl jasmonate vapor. MyAP displayed considerable similarity to an early nodulin (ENOD8) from Medicago sativa and to a proline-rich protein (APG), described as another specific, from Arabidopsis thaliana and B. napus. Similarity to expressed sequence tags from both A. thaliana and Oryza sativa has also been found.

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Selected References

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