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Genetics, Vol 147, 117-123, Copyright © 1997
INVESTIGATIONS |
Schizophyllum commune A{alpha} Mating-Type Proteins, Y and Z, Form Complexes in All Combinations In Vitro
Y. Asada, C. Yue, J. Wu, G. P. Shen, C. P. Novotny and R. C. Ullrich
Departments of Botany and Agricultural Biochemistry, Department of Bioresource Science, Faculty of Agriculture, Kagawa University, Kagawa 761-07 Japan
The A{alpha} locus of the basidiomycete fungus, Schizophyllum commune, regulates sexual development via proteins Y and Z. Each A{alpha} mating type encodes unique Y and Z isoforms. We used two isoforms of Y (Y4 and Y5) and two isoforms of Z (Z4 and Z5) in affinity assays of protein binding. These assays identified two types of protein interactions. Each full-length Y or Z protein binds to itself and other Y or Z proteins regardless of the A{alpha} mating type from which they are encoded (i.e., mating-type independent binding). A second type of binding, detected with partial-length polypeptides, occurs only between N-terminal regions of Y and Z proteins encoded from different A{alpha} mating types (e.g., Y4Z5 or Y5Z4); we refer to this binding as mating-type dependent binding. Deletion analysis shows that the Y4 specificity domain (an N-terminal region conferring recognition uniqueness to the Y4 isoform) is essential for mating-type dependent binding. Other regions of Y and Z are involved in mating-type independent binding. These results, obtained in vitro, raise the possibility that either of several protein complexes composed of Y and/or Z proteins may occur in vivo.
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