Purification, cDNA cloning, and characterization of LysM-containing plant chitinase from horsetail (<i>Equisetum arvense</i>)

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  • Saki Inamine
    Graduate School of Science and Engineering, Kagoshima University, Kagoshima, Japan
  • Shoko Onaga
    Okinawa Prefectural Agricultural Research Center, Itoman, Japan
  • Takayuki Ohnuma
    Department of Advanced Bioscience, Kinki University, Nara, Japan
  • Tamo Fukamizo
    Department of Advanced Bioscience, Kinki University, Nara, Japan
  • Toki Taira
    Department of Bioscience and Biotechnology, University of the Ryukyus, Nishihara-cho, Japan

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<jats:title>Abstract</jats:title> <jats:p>Chitinase-A (EaChiA), molecular mass 36 kDa, was purified from the vegetative stems of a horsetail (Equisetum arvense) using a series of column chromatography. The N-terminal amino acid sequence of EaChiA was similar to the lysin motif (LysM). A cDNA encoding EaChiA was cloned by rapid amplification of cDNA ends and polymerase chain reaction. It consisted of 1320 nucleotides and encoded an open reading frame of 361 amino acid residues. The deduced amino acid sequence indicated that EaChiA is composed of a N-terminal LysM domain and a C-terminal plant class IIIb chitinase catalytic domain, belonging to the glycoside hydrolase family 18, linked by proline-rich regions. EaChiA has strong chitin-binding activity, however, no antifungal activity. This is the first report of a chitinase from Equisetopsida, a class of fern plants, and the second report of a LysM-containing chitinase from a plant.</jats:p>

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