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Two Tcp‐1‐related but highly divergent gene families exist in oat encoding proteins of assumed chaperone function
Author(s) -
Ehmann Bruno,
Krenz Martina,
Mummert Eckart,
Schäfer Eberhard
Publication year - 1993
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(93)80827-h
Subject(s) - complementary dna , biology , chaperone (clinical) , peptide sequence , gene , cdna library , microbiology and biotechnology , coding region , biochemistry , genetics , medicine , pathology
Tcp‐1‐related sequences have been isolated from a cDNA library of etiolated 6‐day‐old oat (Avena sativa) seedlings. This attempt was made to obtain cDNAs of a recently published 60 kDa plant chaperone that re‐folds denatured phytochrome and which was biochemically characterised as a Tcp‐1‐related protein [(1993) Nature 363, 644‐647]. The translation of the putative coding sequence from one full‐length cDNA clone displays no specific homologies to amino acid sequences known from peptide sequencing of the oat 60 kDa chaperone. Antibodies raised against the 60 kDa chaperone and over‐expressed protein from one full‐length coding sequence for Tcp‐1 from oat show no cross‐reactivity, whereas a monoclonal antibody raised against mouse Tcp‐1 protein recognizes both the 60 kDa protein purified from plant extracts and over‐expressed protein from Tcp‐1‐related cDNA sequences.