A proline-rich chitinase from Beta vulgaris

Lars Berglund, Janne Brunstedt, Klaus K Nielsen, Zhaochun Chen, Jørn Dalgaard Mikkelsen, Kjeld Marcker

Research output: Contribution to journalJournal articleResearchpeer-review

Abstract

A gene (Chi) encoding a novel type of chitinase was isolated from Beta vulgaris. The Chi protein consists of an N-terminal hydrophobic prepeptide of 25 amino acids followed by a hevein-like domain of 22 amino acid residues, an unusually long proline-rich domain of 131 amino acid residues with 90 prolines, and finally a catalytic domain of 261 amino acid residues. Proteins with similar proline-rich domains are present in some other plants. The Chl gene shows a transient expression in response to fungal infection.
Original languageEnglish
JournalPlant Molecular Biology
Volume27
Issue number1
Pages (from-to)211-216
ISSN0167-4412
DOIs
Publication statusPublished - 1995
Externally publishedYes

Cite this

Berglund, L., Brunstedt, J., Nielsen, K. K., Chen, Z., Mikkelsen, J. D., & Marcker, K. (1995). A proline-rich chitinase from Beta vulgaris. Plant Molecular Biology, 27(1), 211-216. https://doi.org/10.1007/BF00019193