Isolation of a novel isozyme of tobacco BY-2 chitinase induced by a fungal elicitor

Tomonori Shinya; Kazunari Hanai; Mikako Saito; Hideaki Matsuoka

doi:10.5511/plantbiotechnology.21.155

Isolation of a novel isozyme of tobacco BY-2 chitinase induced by a fungal elicitor

Tomonori Shinya, Kazunari Hanai, Mikako Saito, Hideaki Matsuoka

Research output: Contribution to journal › Article › peer-review

2 Citations (Scopus)

Abstract

Three isozymes of chitinase were induced by a fungal elicitor in cultured tobacco BY-2 cells. The most acidic one, designated TBC-3, was described here. The molecular mass of TBC-3 was estimated to be 28.5 kDa. The N-terminal amino acid sequence of TBC-3 was analyzed and a homology search was performed. Fifteen amino acids at the N-terminus showed 60% homology to class II chitinases from other plants but not higher than 27% homology to already known chitinases from tobacco. Therefore, TBC-3 is thought to be a novel tobacco chitinase that may be classified into class II.

Original language	English
Pages (from-to)	155-158
Number of pages	4
Journal	Plant Biotechnology
Volume	21
Issue number	2
DOIs	https://doi.org/10.5511/plantbiotechnology.21.155
Publication status	Published - Jun 2004
Externally published	Yes

Keywords

Alternaria alternata
Amino acid sequence homology
Chitinase isozyme
Tobacco BY-2 cells

ASJC Scopus subject areas

Biotechnology
Agronomy and Crop Science
Plant Science

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title = "Isolation of a novel isozyme of tobacco BY-2 chitinase induced by a fungal elicitor",

abstract = "Three isozymes of chitinase were induced by a fungal elicitor in cultured tobacco BY-2 cells. The most acidic one, designated TBC-3, was described here. The molecular mass of TBC-3 was estimated to be 28.5 kDa. The N-terminal amino acid sequence of TBC-3 was analyzed and a homology search was performed. Fifteen amino acids at the N-terminus showed 60% homology to class II chitinases from other plants but not higher than 27% homology to already known chitinases from tobacco. Therefore, TBC-3 is thought to be a novel tobacco chitinase that may be classified into class II.",

keywords = "Alternaria alternata, Amino acid sequence homology, Chitinase isozyme, Tobacco BY-2 cells",

author = "Tomonori Shinya and Kazunari Hanai and Mikako Saito and Hideaki Matsuoka",

year = "2004",

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doi = "10.5511/plantbiotechnology.21.155",

language = "English",

volume = "21",

pages = "155--158",

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T1 - Isolation of a novel isozyme of tobacco BY-2 chitinase induced by a fungal elicitor

AU - Shinya, Tomonori

AU - Hanai, Kazunari

AU - Saito, Mikako

AU - Matsuoka, Hideaki

PY - 2004/6

Y1 - 2004/6

N2 - Three isozymes of chitinase were induced by a fungal elicitor in cultured tobacco BY-2 cells. The most acidic one, designated TBC-3, was described here. The molecular mass of TBC-3 was estimated to be 28.5 kDa. The N-terminal amino acid sequence of TBC-3 was analyzed and a homology search was performed. Fifteen amino acids at the N-terminus showed 60% homology to class II chitinases from other plants but not higher than 27% homology to already known chitinases from tobacco. Therefore, TBC-3 is thought to be a novel tobacco chitinase that may be classified into class II.

AB - Three isozymes of chitinase were induced by a fungal elicitor in cultured tobacco BY-2 cells. The most acidic one, designated TBC-3, was described here. The molecular mass of TBC-3 was estimated to be 28.5 kDa. The N-terminal amino acid sequence of TBC-3 was analyzed and a homology search was performed. Fifteen amino acids at the N-terminus showed 60% homology to class II chitinases from other plants but not higher than 27% homology to already known chitinases from tobacco. Therefore, TBC-3 is thought to be a novel tobacco chitinase that may be classified into class II.

KW - Alternaria alternata

KW - Amino acid sequence homology

KW - Chitinase isozyme

KW - Tobacco BY-2 cells

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JO - Plant Biotechnology

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Isolation of a novel isozyme of tobacco BY-2 chitinase induced by a fungal elicitor

Abstract

Keywords

ASJC Scopus subject areas

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