Premium
Structure and organ specificity of an anionic peroxidase from Arabidopsis thaliana cell suspension culture
Author(s) -
Østergaard Lars,
Abelskov Anne Katrine,
Mattsson Ole,
Welinder Karen G.
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(96)01244-6
Subject(s) - horseradish peroxidase , complementary dna , arabidopsis , arabidopsis thaliana , microbiology and biotechnology , peroxidase , biology , cdna library , biochemistry , signal peptide , clone (java method) , chemistry , gene , peptide sequence , enzyme , mutant
The predominant peroxidase (pl 3.5) (E.C. 1.11.1.7) of an Arabidopsis thaliana cell suspension culture was purified and partially sequenced. Oligonucleotides were designed and a specific probe was obtained. A cDNA clone was isolated from an Arabidopsis cell suspension cDNA library and completely sequenced. The cDNA clone comprised 1194 bp and encodes a 30 residue signal peptide and a 305 residue mature protein ( M r 31 966). The sequence of the mature protein is 95% identical to the well‐characterized horseradish peroxidase HRP A2 and has therefore been designated ATP A2. Three introns at positions identical to those found in Arabidopsis and horseradish genes encoding cationic peroxidases were identified. RT‐PCR analysis revealed root‐specific expression.