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J. Cell Biol.,
Volume 141, Number 5, June 1, 1998 1217-1228
* Department of Genetics, Institute of Molecular Biology, ØsterFarimagsgade 2A, University of Copenhagen, DK-1353
Copenhagen K, Denmark; and Formins are involved in diverse aspects of
morphogenesis, and share two regions of homology:
FH1 and FH2. We describe a new formin homology region, FH3. FH3 is an amino-terminal domain that differs from the Rho binding site identified in Bni1p and
p140mDia. The Schizosaccharomyces pombe formin
Fus1 is required for conjugation, and is localized to the
projection tip in cells of mating pairs. We replaced genomic fus1+ with green fluorescent protein (GFP)-
tagged versions that lacked either the FH1, FH2, or
FH3 domain. Deletion of any FH domain essentially
abolished mating. FH3, but neither FH1 nor FH2, was required for Fus1 localization. An FH3 domain-GFP
fusion protein localized to the projection tips of mating
pairs. Thus, the FH3 domain alone can direct protein
localization. The FH3 domains of both Fus1 and the S. pombe cytokinesis formin Cdc12 were able to localize
GFP to the spindle pole body in half of the late G2 cells
in a vegetatively growing population. Expression of
both FH3-GFP fusions also affected cytokinesis. Overexpression of the spindle pole body component Sad1 altered the distribution of both Sad1 and the FH3-GFP
domain. Together these data suggest that proteins at
multiple sites can interact with FH3 domains.
School of Biological Sciences, University of Manchester, Manchester M13 9PT, United Kingdom
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