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note
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-6 M was added for 2 hours. Cells were harvested by centrifugation, resuspended in buffer TNE450 [50 mM Tris-HCl (pH 7.5), 450 mM NaCl, 10 mM EDTA, and 0.1% NP-40] and broken with glass beads in a Mini Beadbeater (Biospec). After two sequential centrifugations, the supernatant was incubated for 1 hour with protein G-sepharose beads (Pharmacia) covalently coupled to polyoma antibodies (39). Beads were washed three times with buffer TNE450 and twice with binding buffer [10 mM Tris-HCl (pH 7.5), 85 mM NaCl, 10 mM EDTA, 0.1 % NP-40]. The beads were then divided into aliquots and incubated for 30 min at 4°C with Bem1p-6His purified from E. coli (11). The beads were washed three times with binding buffer and Far1p was then specifically eluted with binding buffer containing 10 μM polyoma peptide (EYMPME) and 0.1% N-octylglucoside (Fluka). Bound Bem1p-6His was detected by immunoblotting using polyclonal antibodies against Bem1p (12).
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31
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3643056750
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note
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4 (pH 7.3)]. Bound proteins were eluted with gel-sample buffer and subjected to immunoblot analysis with polyclonal antibodies against Far1p and Cdc24p. Polyclonal antibodies against Cdc24p were raised against a MalE-Cdc24 fusion protein (kindly provided by E. Bi) and affinity purified as described (39). Coimmunoprecipitation experiments with Far1p and Ste4p were carried out as above, except that YMP290 cells were transformed with plasmids expressing Far1p (ACB435) (40) and either epitope-tagged HA-Ste4p (pYEE181) (13) or untagged Ste4p (pTP288) from the inducible GAL promoter. HA11-immunoprecipitates were immunoblotted with polyclonal antibodies against Far1p and Ste4p.
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1-389). All strains were constructed by single-step gene replacement (37) using the plasmid pTP4 digested with Not I (31); successful replacement of the endogenous FAR1 locus by far1-c was confirmed by the appearance of truncated Far1-c protein by immunoblotting. Mating assays were carried out with the mating tester IH1793 as described (21). In contrast to double mutants between far1-c and proteins functioning in the default mating pathway (such as Pea2p) (5), far1-c cdcZ4-m double mutants mate with an efficiency comparable to each single mutant.
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34
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3643130837
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1-389 corresponds to Far1p-c (31). The PCR fragment amplified with the primer pair oTP418/oTP404 digested with Not I and Xho I was also ligated into pEG203 to yield plasmid ACB414. Constructs lacking the RING finger domain (amino acids 203 to 284) or the Ste5p homology domain (amino acids 440 to 531) were constructed by site-directed mutagenesis using the ExSite kit as recommended by the manufacturer (Stratagene); the introduced mutations were confirmed by sequencing. The fragments were cloned into pJC4-6 for two-hybrid analysis (generating plasmids pTP524 and ACB421) or PRD53 (generating plasmids pTP525 and pKP7) for mating assays. Genomic DNA isolated from strains IH2640 and IH2637 (5) was used to amplify the coding sequences of the far1-s alleles H7 and B4 by PCR using the primers oTP410 and oTP404. The obtained fragments were digested with Nco I and Xho I and ligated into pJG4-6 for two-hybrid analysis to generate plasmids ACB425 and ACB426. Expression of all Far1 mutants and fusion proteins was controlled by immunoblotting with Far1p-specific antibodies.
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35
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0030465534
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-6 M α factor to 3 ml of log phase cultures at 30°C. Cells were sonicated, fixed with formaldehyde to a final concentration of 3.7%, and viewed by differential interference microscopy. Yeast actin was visualized with rhodaminephalloidin (Molecular Probes, Eugene, OR) as described previously [M. Peter, A. M. Neiman, H.-O. Park, M. van Lohuizen, I. Herskowitz, EMBO J. 15, 7046 (1996)].
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1-389-GFP expressed from the GAL promoter were present at similar levels in cells treated or not treated with α factor. GFP fluorescence was visualized on a Zeiss Axiovert 100 microscope equipped with a Chroma GFPII filter (excitation at 470 to 440 nm wavelength) and photographed with a Photometrics CCD (charge-coupled device) camera as described [M. Jaquenoud, M.-P. Gulli, K. Peter, M. Peter, EMBO J. 17, 5360 (1998)). Immunofluorescence experiments using Far1p fused to three copies of the myc epitope confirmed that, in the absence of pheromones, Far1p is localized in the nucleus, whereas in pheromone treated cells, Far1p is found predominantly in the cytosol.
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note
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We thank members of each laboratory for helpful discussions; C. Boone, R. A. Arkowitz, J. Chant, D. Lew, M. Funk, E. Elion, E. O'Shea, H.-O. Park, E. Bi, and E. Leberer for plasmids and strains; B. Catarin for polyclonal antibodies to Far1p; and E. Leberer for antibodies to Bem1p. We also thank N. Valtz, S. Henchoz and K. Peter for help during early aspects of this work and J. Philips, V. Simanis, and R. Iggo for critical reading of the manuscript. L.S.H. was supported by an NIH postdoctoral fellowship. Work in the I.H. laboratory was supported by an NIH research grant (GM48052). P.M.P. is supported by grants from the Worcester Foundation, the Millipore Foundation, and NIH (GM57769). M.P. is supported by the Swiss National Science Foundation, the Swiss Cancer League, and a Helmut Horten Incentive award. I.H. dedicates this paper to J. Stahl.
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