title: Membrane organization and cell fusion during mating in fission yeast requires multipass membrane protein Prm1.
abstract: The involvement of Schizosaccharomyces pombe prm1(+) in cell fusion during mating and its relationship with other genes required for this process have been addressed. S. pombe prm1Δ mutant exhibits an almost complete blockade in cell fusion and an abnormal distribution of the plasma membrane and cell wall in the area of cell-cell interaction. The distribution of cellular envelopes is similar to that described for mutants devoid of the Fig1-related claudin-like Dni proteins; however, prm1(+) and the dni(+) genes act in different subpathways. Time-lapse analyses show that in the wild-type S. pombe strain, the distribution of phosphatidylserine in the cytoplasmic leaflet of the plasma membrane undergoes some modification before an opening is observed in the cross wall at the cell-cell contact region. In the prm1Δ mutant, this membrane modification does not take place, and the cross wall between the mating partners is not extensively degraded; plasma membrane forms invaginations and fingers that sometimes collapse/retract and that are sometimes strengthened by the synthesis of cell-wall material. Neither prm1Δ nor prm1Δ dniΔ zygotes lyse after cell-cell contact in medium containing and lacking calcium. Response to drugs that inhibit lipid synthesis or interfere with lipids is different in wild-type, prm1Δ, and dni1Δ strains, suggesting that membrane structure/organization/dynamics is different in all these strains and that Prm1p and the Dni proteins exert some functions required to guarantee correct membrane organization that are critical for cell fusion.
authors: Departamento de Microbiología y Genética/Instituto de Biología Funcional y Genómica, Universidad de Salamanca/Consejo Superior de Investigaciones Científicas, 37007 Salamanca, Spain.
authors: M-Ángeles
authors: MÁ
authors: Curto
authors: Mohammad Reza
authors: MR
authors: Sharifmoghadam
authors: Eduardo
authors: E
authors: Calpena
authors: Nagore
authors: N
authors: De León
authors: Marta
authors: M
authors: Hoya
authors: Cristina
authors: C
authors: Doncel
authors: Janet
authors: J
authors: Leatherwood
authors: M-Henar
authors: MH
authors: Valdivieso
mesh_terms: D002462:Cell Membrane / Q000378:metabolism* / Q000648:ultrastructure; D002473:Cell Wall / Q000378:metabolism* / Q000648:ultrastructure; D047630:Depsipeptides / Q000494:pharmacology; D005229:Fatty Acids, Monounsaturated / Q000378:metabolism; D015966:Gene Expression Regulation, Fungal; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism*; D008825:Miconazole / Q000494:pharmacology; D008954:Models, Biological; D012568:Schizosaccharomyces / Q000166:cytology / Q000254:growth & development / Q000648:ultrastructure*; D029702:Schizosaccharomyces pombe Proteins / Q000235:genetics / Q000378:metabolism*
chemical_list: D047630:Depsipeptides; C000594912:Dni1 protein, S pombe; D005229:Fatty Acids, Monounsaturated; D008565:Membrane Proteins; C000594911:Prm1 protein, S pombe; D029702:Schizosaccharomyces pombe Proteins; C474171:papuamide B; D008825:Miconazole; C001996:thermozymocidin
keywords: Prm1; cell fusion; mating; membrane; yeast