Structure and organ specificity of an anionic peroxidase from Arabidopsis thaliana cell suspension culture

FEBS Letters

Welinder, Karen G.¹  Østergaard, Lars¹  Abelskov, Anne Katrine¹  Mattsson, Ole² 

[1] Department of Protein Chemistry, Institute of Molecular Biology, University of Copenhagen, Øster Farimagsgade 2A, DK-1353 Copenhagen K, Denmark;Department of Plant Physiology, Institute of Molecular Biology, University of Copenhagen, Øster Farimagsgade 2A, DK-1353 Copenhagen K, Denmark

关键词: Anionic peroxidase;    Arabidopsis thaliana;    Plant cDNA;    Peroxidase structure;    Root specificity;   

DOI  :  10.1016/S0014-5793(96)01244-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown