Sa. Young et al., RICE CATIONIC PEROXIDASE ACCUMULATES IN XYLEM VESSELS DURING INCOMPATIBLE INTERACTIONS WITH XANTHOMONAS-ORYZAE PV ORYZAE, Plant physiology, 107(4), 1995, pp. 1333-1341
A cationic peroxidase, PO-C1 (molecular mass 42 kD, isoelectric point
8.6), which is induced in incompatible interactions between the vascul
ar pathogen Xanthomonas oryzae pv oryzae and rice (Oryza sativa L.), w
as purified. Amino acid sequences from chemically cleaved fragments of
PO-C1 exhibited a high percentage of identity with deduced sequences
of peroxidases from rice, barley, and wheat. Polyclonal antibodies wer
e raised to an 11-amino acid oligopeptide (POC1a) that was derived fro
m a domain where the sequence of the cationic peroxidase diverged from
other known peroxidases. The anti-POC1a antibodies reacted only with
a protein of the same mobility as PO-C1 in extracellular and guttation
fluids from plants undergoing incompatible responses collected at 24
h after infection. In the compatible responses, the antibodies did not
detect PO-C1 until 48 h after infection. Immunoelectron microscopy wa
s used to demonstrate that PO-C1 accumulated within the apoplast of me
sophyll cells and within the cell walls and vessel lumen of xylem elem
ents of plants undergoing incompatible interactions.