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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
Author(s) -
Gus-Mayer Sabine,
Brunner Harald,
Schneider-Poetsch Hansjörg A.W.,
Lottspeich Friedrich,
Eckerskorn Christoph,
Grimm Rudolf,
Rüdiger Wolfhart
Publication year - 1994
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 - 10.1016/0014-5793(94)00503-6
Subject(s) - complementary dna , peptide sequence , biology , biochemistry , phytochrome , chaperone (clinical) , amino acid , protein kinase a , microbiology and biotechnology , kinase , gene , botany , medicine , red light , pathology
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.