The amino acid sequence previously attributed to a protein kinase or a TCP1‐related molecular chaperone and co‐purified with phytochrome is a β‐glucosidase

FEBS Letters

Gus-Mayer, Sabine¹  Rüdiger, Wolfhart¹  Eckerskorn, Christoph⁴  Lottspeich, Friedrich⁴  Grimm, Rudolf²  Schneider-Poetsch, Hansjörg A.W.³  Brunner, Harald¹ 

[1]Botanisches Institut, Universität München, Menzinger Straße 67, D-80638 München, Germany

[2]Hewlett Packard GmbH, Hewlett-Packard-Straße 8, D-76337 Waldbronn, Germany

[3]Botanisches Institut der Universität zu Köln, Gyrhofstraße 15, D-50931 Köln, Germany

[4]Max-Planck-Institut für Biochemie, Am Klopferspitz 18a, D-82152 Martinsried, Germany

关键词: Avena sativa;    Avenacosidase;    β-Glucosidase aggregate;    Phytochrome;    TCP1;    t-complex polypeptide-1;    P60;    60 kDa protein with β-glucosidase activity;    HPLC;    high-performance liquid chromatography;    PAGE;    polyacrylamide gel electrophoresis;    K;    kilodalton;    cpn60;    60 kDa plant chloroplast chaperonin;    GroEL;    60 kDa prokaryotic cytosol chaperone.;   

DOI  :  10.1016/0014-5793(94)00503-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A 60 kDa protein (P60) co-purified with phytochrome was identified as avenacosidase, a β-glucosidase which is part of the defense system of Avena sativa. An antiserum raised against P60 was used to isolate a cDNA clone coding for the complete amino acid sequence of P60. The cDNA-derived amino acid sequence contained the partial sequences described before for a protein kinase [(1989) Planta 178, 199–206] and for a TCP1-related molecular chaperone [(1993) Nature 363, 644–647] co-purified with phytochrome. We conclude that these activities were related to minor contaminants and that only sequences of avenacosidase had been obtained.

【 授权许可】

Unknown