Abstract
Summary Screening of an expression cDNA library from Chlamydomonas reinhardtii with the monoclonal antibody Z-3 B1 directed against phytochrome from Zea mays yielded the positive clone «ZBI». The clone consists of 874 base pairs containing an open reading frame of 209 amino acids. The sequence has no homology with any phytochrome sequence but a remote homology with ubiH of Escherichia coli , which is supposed to be a flavoprotein (Nakahigashi et al., J. Bacteriol. 174, 7352-7359, 1992). Since the epitope for Z-3 B1 previously mapped in oat phytochrome (Bonenberger et al., Photochem. Photobiol. 56, 717723, 1992) is not contained in the sequence of ZBI, subclones of ZBI were prepared, expressed as fusion proteins and tested for reaction against the monoclonal antibody Z-3B1. By computer-aided folding of the peptide chain, a «composed epitope* was deduced that has sufficient homology with the authentic epitope in order to create cross-reactivity. Results obtained by heterologous screening with monoclonal antibodies have to be interpreted with caution.
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