Originally published as Genetics Published Articles Ahead of Print on December 1, 2005.

Genetics, Vol. 172, 873-884, February 2006, Copyright © 2006
doi:10.1534/genetics.105.045542

An Essential Gene for Fruiting Body Initiation in the Basidiomycete Coprinopsis cinerea Is Homologous to Bacterial Cyclopropane Fatty Acid Synthase Genes

Yi Liu^*,1, Prayook Srivilai, Sabine Loos^*,2, Markus Aebi^* and Ursula Kües^,3

^* Institute for Microbiology, ETH Zurich, CH-8093 Zurich, Switzerland and Molecular Wood Biotechnology, Institute for Forest Botany, Georg-August University, D-37077 Göttingen, Germany

³ Corresponding author: Georg-August University Göttingen, Institute for Forest Botany, Section Molecular Wood Biotechnology, Büsgenweg 2, D-37077 Göttingen, Germany.
E-mail: ukuees{at}gwdg.de

The self-compatible Coprinopsis cinerea homokaryon AmutBmut produces fruiting bodies without prior mating to another strain. Early stages of fruiting body development include the dark-dependent formation of primary hyphal knots and their light-induced transition to the more compact secondary hyphal knots. The AmutBmut UV mutant 6-031 forms primary hyphal knots, but development arrests at the transition state by a recessive defect in the cfs1 gene, isolated from a cosmid library by mutant complementation. A normal primordia phenotype was achieved when cfs1⁺ was embedded at both sides in at least 4.0 kb of native flanking DNA. Truncations of the flanking DNA lead to reduction in transformation frequencies and faults in primordia tissue formation, suggesting that the gene is also acting at later stages of development. The cfs1 gene encodes a protein highly similar to cyclopropane fatty acid synthases, a class of enzymes shown in prokaryotes and recently in a plant to convert membrane-bound unsaturated fatty acids into cyclopropane fatty acids. In C. cinerea 6-031, the mutant cfs1 allele carries a T-to-G transversion, leading to an amino acid substitution (Y441D) in a domain suggested to be involved in the catalytic function of the protein and/or membrane interaction.

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