Accumulation of defence-related transcripts and cloning of a chitinase mRNA from pea leaves (Pisum sativum L.) inoculated with Ascochyta pisi Lib.

TY - JOUR

T1 - Accumulation of defence-related transcripts and cloning of a chitinase mRNA from pea leaves (Pisum sativum L.) inoculated with Ascochyta pisi Lib.

AU - Vad, Knud

AU - de Neergaard, Eigil

AU - Madriz-Ordeñana, Kenneth

AU - Mikkelsen, Jørn D.

AU - Collinge, David B.

PY - 1993

Y1 - 1993

N2 - The race specific resistance of pea to Ascochyta pisi Lib. was shown to be exhibited as a hypersensitive response associated with the production of polyphenolic substances in epidermal and mesophyll cells. The levels of transcripts representing a pathogenesis-related (PR) protein (chitinase) and an enzyme of phytoalexin biosynthesis (chalcone synthase) were shown to accumulate more rapidly during the hypersensitive response than during lesion development in the compatible interaction. A full-length (1143 bp) cDNA sequence of a pea chitinase (EC 3.2.1.14) (coding for an approx. 34 500 Da protein) was deduced by combining the overlapping sequences of three clones obtained following PCR amplification of cDNA prepared from mRNA isolated 24 h after inoculation of pea leaves with Ascochyta pisi. The combined sequences were identified as a class I chitinase corresponding to the basic A1-chitinase enzyme previously isolated from pea leaves (Vad et al., Planta, 184 (1991) 24-29). Like class III and IV chitinases, the pea sequence differs from other class I chitinases in the absence of a hydrophobic C-terminal domain. © 1993.

AB - The race specific resistance of pea to Ascochyta pisi Lib. was shown to be exhibited as a hypersensitive response associated with the production of polyphenolic substances in epidermal and mesophyll cells. The levels of transcripts representing a pathogenesis-related (PR) protein (chitinase) and an enzyme of phytoalexin biosynthesis (chalcone synthase) were shown to accumulate more rapidly during the hypersensitive response than during lesion development in the compatible interaction. A full-length (1143 bp) cDNA sequence of a pea chitinase (EC 3.2.1.14) (coding for an approx. 34 500 Da protein) was deduced by combining the overlapping sequences of three clones obtained following PCR amplification of cDNA prepared from mRNA isolated 24 h after inoculation of pea leaves with Ascochyta pisi. The combined sequences were identified as a class I chitinase corresponding to the basic A1-chitinase enzyme previously isolated from pea leaves (Vad et al., Planta, 184 (1991) 24-29). Like class III and IV chitinases, the pea sequence differs from other class I chitinases in the absence of a hydrophobic C-terminal domain. © 1993.

KW - Chalcone synthase

KW - Extensin

KW - Hydrolase (antifungal)

KW - Hypersensitive response

KW - Pathogenesis-related protein

KW - Polymerase chain reaction

U2 - 10.1016/0168-9452(93)90067-A

DO - 10.1016/0168-9452(93)90067-A

M3 - Journal article

SN - 0168-9452

VL - 92

SP - 69

EP - 79

JO - Plant Science

JF - Plant Science

IS - 1

ER -