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cdc12p, a protein required for cytokinesis in fission yeast, is a component of the cell division ring and interacts with profilin.

Chang F, Drubin D, Nurse P - J. Cell Biol. (1997)

Bottom Line: Here we show that cdc12p is a member of a family of proteins including Drosophila diaphanous, Saccharomyces cerevisiae BNI1, and S. pombe fus1, which are involved in cytokinesis or other actin-mediated processes.Based on these patterns, we present a model in which ring assembly originates from a single point on the cortex and in which a molecular pathway for the functions of cytokinesis proteins is suggested.Finally, we found that cdc12 and cdc3 mutants show a synthetic-lethal genetic interaction, and a proline-rich domain of cdc12p binds directly to profilin cdc3p in vitro, suggesting that one function of cdc12p in ring assembly is to bind profilin.

View Article: PubMed Central - PubMed

Affiliation: Imperial Cancer Research Fund, London, United Kingdom. fc99@columbia.edu

ABSTRACT
As in many other eukaryotic cells, cell division in fission yeast depends on the assembly of an actin ring that circumscribes the middle of the cell. Schizosaccharomyces pombe cdc12 is an essential gene necessary for actin ring assembly and septum formation. Here we show that cdc12p is a member of a family of proteins including Drosophila diaphanous, Saccharomyces cerevisiae BNI1, and S. pombe fus1, which are involved in cytokinesis or other actin-mediated processes. Using indirect immunofluorescence, we show that cdc12p is located in the cell division ring and not in other actin structures. When overexpressed, cdc12p is located at a medial spot in interphase that anticipates the future ring site. cdc12p localization is altered in actin ring mutants. cdc8 (tropomyosin homologue), cdc3 (profilin homologue), and cdc15 mutants exhibit no specific cdc12p staining during mitosis. cdc4 mutant cells exhibit a medial cortical cdc12p spot in place of a ring. mid1 mutant cells generally exhibit a cdc12p spot with a single cdc12p strand extending in a random direction. Based on these patterns, we present a model in which ring assembly originates from a single point on the cortex and in which a molecular pathway for the functions of cytokinesis proteins is suggested. Finally, we found that cdc12 and cdc3 mutants show a synthetic-lethal genetic interaction, and a proline-rich domain of cdc12p binds directly to profilin cdc3p in vitro, suggesting that one function of cdc12p in ring assembly is to bind profilin.

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cdc3 and cdc12 exhibit a synthetic-lethal genetic interaction. Siblings from a tetratype tetrad in a cross between cdc3-313  and cdc12-112 mutants were streaked on YE5S plates and incubated at 25°, 29°, or 36°C. Growth was assayed by colony formation. Note that the cdc3 cdc12 double mutant exhibited markedly  reduced growth at 25° and 29°C where the single mutants are viable. Strains were FC322 (cdc12-112), FC323 (wt), FC324 (cdc3313), and FC325 (cdc3-313 cdc12-112).
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Figure 8: cdc3 and cdc12 exhibit a synthetic-lethal genetic interaction. Siblings from a tetratype tetrad in a cross between cdc3-313 and cdc12-112 mutants were streaked on YE5S plates and incubated at 25°, 29°, or 36°C. Growth was assayed by colony formation. Note that the cdc3 cdc12 double mutant exhibited markedly reduced growth at 25° and 29°C where the single mutants are viable. Strains were FC322 (cdc12-112), FC323 (wt), FC324 (cdc3313), and FC325 (cdc3-313 cdc12-112).

Mentions: First, we tested whether cdc3 and cdc12 interact genetically by constructing cdc12 and cdc3 double mutants. Fig. 8 shows the phenotypes of wild-type, cdc3, cdc12, and cdc3 cdc12 mutants. The cdc3-313 cdc12-112 double mutants had a much more severe phenotype than either single mutant. cdc3 cdc12 mutant spores were either dead at 25°C or produced cells with very poor growth at 25°C and no growth at the intermediate temperature of 29°C. In comparison, single cdc3 and cdc12 mutants grew well at 25°C and 29°C. The single mutants and the double mutants did not grow at 36°C. Thus, cdc3 and cdc12 genes exhibit a synthetic-lethal interaction, which suggests that these gene products may interact at some level in vivo.


cdc12p, a protein required for cytokinesis in fission yeast, is a component of the cell division ring and interacts with profilin.

Chang F, Drubin D, Nurse P - J. Cell Biol. (1997)

cdc3 and cdc12 exhibit a synthetic-lethal genetic interaction. Siblings from a tetratype tetrad in a cross between cdc3-313  and cdc12-112 mutants were streaked on YE5S plates and incubated at 25°, 29°, or 36°C. Growth was assayed by colony formation. Note that the cdc3 cdc12 double mutant exhibited markedly  reduced growth at 25° and 29°C where the single mutants are viable. Strains were FC322 (cdc12-112), FC323 (wt), FC324 (cdc3313), and FC325 (cdc3-313 cdc12-112).
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Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC2139860&req=5

Figure 8: cdc3 and cdc12 exhibit a synthetic-lethal genetic interaction. Siblings from a tetratype tetrad in a cross between cdc3-313 and cdc12-112 mutants were streaked on YE5S plates and incubated at 25°, 29°, or 36°C. Growth was assayed by colony formation. Note that the cdc3 cdc12 double mutant exhibited markedly reduced growth at 25° and 29°C where the single mutants are viable. Strains were FC322 (cdc12-112), FC323 (wt), FC324 (cdc3313), and FC325 (cdc3-313 cdc12-112).
Mentions: First, we tested whether cdc3 and cdc12 interact genetically by constructing cdc12 and cdc3 double mutants. Fig. 8 shows the phenotypes of wild-type, cdc3, cdc12, and cdc3 cdc12 mutants. The cdc3-313 cdc12-112 double mutants had a much more severe phenotype than either single mutant. cdc3 cdc12 mutant spores were either dead at 25°C or produced cells with very poor growth at 25°C and no growth at the intermediate temperature of 29°C. In comparison, single cdc3 and cdc12 mutants grew well at 25°C and 29°C. The single mutants and the double mutants did not grow at 36°C. Thus, cdc3 and cdc12 genes exhibit a synthetic-lethal interaction, which suggests that these gene products may interact at some level in vivo.

Bottom Line: Here we show that cdc12p is a member of a family of proteins including Drosophila diaphanous, Saccharomyces cerevisiae BNI1, and S. pombe fus1, which are involved in cytokinesis or other actin-mediated processes.Based on these patterns, we present a model in which ring assembly originates from a single point on the cortex and in which a molecular pathway for the functions of cytokinesis proteins is suggested.Finally, we found that cdc12 and cdc3 mutants show a synthetic-lethal genetic interaction, and a proline-rich domain of cdc12p binds directly to profilin cdc3p in vitro, suggesting that one function of cdc12p in ring assembly is to bind profilin.

View Article: PubMed Central - PubMed

Affiliation: Imperial Cancer Research Fund, London, United Kingdom. fc99@columbia.edu

ABSTRACT
As in many other eukaryotic cells, cell division in fission yeast depends on the assembly of an actin ring that circumscribes the middle of the cell. Schizosaccharomyces pombe cdc12 is an essential gene necessary for actin ring assembly and septum formation. Here we show that cdc12p is a member of a family of proteins including Drosophila diaphanous, Saccharomyces cerevisiae BNI1, and S. pombe fus1, which are involved in cytokinesis or other actin-mediated processes. Using indirect immunofluorescence, we show that cdc12p is located in the cell division ring and not in other actin structures. When overexpressed, cdc12p is located at a medial spot in interphase that anticipates the future ring site. cdc12p localization is altered in actin ring mutants. cdc8 (tropomyosin homologue), cdc3 (profilin homologue), and cdc15 mutants exhibit no specific cdc12p staining during mitosis. cdc4 mutant cells exhibit a medial cortical cdc12p spot in place of a ring. mid1 mutant cells generally exhibit a cdc12p spot with a single cdc12p strand extending in a random direction. Based on these patterns, we present a model in which ring assembly originates from a single point on the cortex and in which a molecular pathway for the functions of cytokinesis proteins is suggested. Finally, we found that cdc12 and cdc3 mutants show a synthetic-lethal genetic interaction, and a proline-rich domain of cdc12p binds directly to profilin cdc3p in vitro, suggesting that one function of cdc12p in ring assembly is to bind profilin.

Show MeSH
Related in: MedlinePlus