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Comparative Study
. 1994 Jun 20;347(1):51-4.
doi: 10.1016/0014-5793(94)00503-6.

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

S Gus-Mayer  1 , H Brunner, H A Schneider-Poetsch, F Lottspeich, C Eckerskorn, R Grimm, W Rüdiger
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Free article
Comparative Study

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

S Gus-Mayer et al. FEBS Lett. .
Free article

Abstract

A 60 kDa protein (P60) co-purified with phytochrome was identified as avenacosidase, a beta-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.

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