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  • 1
    Electronic Resource
    Electronic Resource
    The KlFUS1 gene is required for proper haploid mating and its expression is enhanced by the active form of the Gα (Gpa1) subunit involved in the pheromone response pathway of the yeast Kluyveromyces lactis (2003)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 219 (2003), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The Kluyveromyces lactis FUS1 gene was cloned, physically characterized and its role in the mating response pathway was determined. The gene encodes a putative membrane protein, whose structure shows a single membrane-spanning segment, a short extracellular amino-terminus and a long carboxy-terminus, located in the cytoplasmic side. The predicted primary structure of the protein shows a number of serine and threonine residues in the amino-terminus, which in analogy to Fus1p of Saccharomyces cerevisiae might be O-glycosylated. A fus1-GFP hybrid protein was tentatively located in the plasma membrane of dividing cells and upon activation of the pheromone response pathway, the protein seems to be relocated at the tip of elongated cells. KlFus1p is required for optimal conjugation of sexual partners and its expression is significantly enhanced by overexpression of both a constitutively active form of KlGpa1p, the G protein α subunit that triggers the mating response in this strain, and the KlSte12p transcription factor. Inactivation of the KlSte12 protein strongly reduces mating and affects KlFUS1 gene expression. The KlFUS1 gene has been deposited in the GenBank under accession number AF519444.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/S0378-1097(02)01202-8
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  • 2
    Electronic Resource
    Electronic Resource
    The carboxy-terminal tail of the Ste2 receptor is involved in activation of the G protein in the Saccharomyces cerevisiaeα-pheromone response pathway (2001)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 197 (2001), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The Ste2 gene encodes the yeast α-pheromone receptor that belongs to the superfamily of seven-transmembrane G protein-coupled receptors. Binding of pheromone induces activation of the heterotrimeric G protein triggering growth arrest in G1 phase and induction of genes required for mating. By random PCR-mediated mutagenesis we isolated mutant 8L4, which presents a substitution of an asparagine residue by serine at position 388 of the α-factor receptor. The 8L4 mutant strain shows phenotypic defects such as: reduction in growth arrest after pheromone treatment, diminished activation of the Fus1 gene, and impaired mating competence. The asparagine residue lies in the second half of the intracellular protruding C-terminal tail of the receptor, and its replacement by serine affects interaction with both the Gα and Gβ subunits. Since expression of the receptor as well as its kinetic parameters, i.e., ligand affinity and receptor number, are unaffected in the mutant strain, we propose that association of the C-terminal tail of the receptor with Gα and Gβ subunits is required for proper activation of the heterotrimeric G protein. Besides its described role in downregulation and in formation of preactivation complex, the results here shown indicate that the C-terminal tail of the receptor plays an active role in transmitting the stimulus of mating pheromone to the heterotrimeric G protein.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.2001.tb10584.x
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  • 3
    Electronic Resource
    Electronic Resource
    Nucleotide sequence and chromosomal localization of the gene encoding the old yellow enzyme from Kluyveromyces lactis (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 11 (1995), S. 459-465 
    Details
    ISSN: 0749-503X
    Keywords: Old Yellow Enzyme ; flavoproteins ; Kluyveromyces lactis ; chromosome mapping ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: A 6·6 kb genomic DNA fragment from the yeast Kluyveromyces lactis was isolated. Sequence analysis of this fragment revealed the presence of two incomplete open reading frames (ORFs) in one strand, one coding for the carboxyl terminus of the plasma membrane H+-ATPase and the other for the amino terminus of an unidentified product. In the complementary strand, a full-length ORF which encodes for a protein homologous to the yeast NADPH-dependent Old Yellow Enzyme was found. The deduced amino acid sequence of this ORF predicts a protein of 398 residues with 84% similarity in its full length to OYE1 from Saccharomyces carlsbergensis and OYE2 from Saccharomyces cerevisiae. In addition, an internal region showed considerable similarity to the bile acid-inducible polypeptide from Eubacterium sp., to the NADH oxidase from Thermoanaerobium brockii, to the trimethylamino dehydrogenase from bacterium W3A1 and to the estrogen-binding protein from Candida albicans, suggesting a functional or structural relationship between them. Inactivation of the KYE1 (Kluyveromyces Yellow Enzyme) gene by deletion of 0·6 kb fragment between positions +358 and +936 produced viable cells with a slight increase in their generation time. Haploid cells carrying the disrupted allele showed one-third of the NADPH oxidase activity, compared to wild-type cells. Southern blotting analysis of digested DNA and chromosomes separated by contour-clamped homogeneous electric field electrophoresis from K. lactis indicated that this is a single-copy gene and it is localized on chromosome II, whose molecular size has been estimated to be approximately 1·3 Mb. The sequence reported in this paper has been deposited in the GenBank data base (Accession No. L37452).
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320110509
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  • 4
    Electronic Resource
    Electronic Resource
    Separate roles for N- and C-termini of the STE4 (β) subunit of the Saccharomyces cerevisiae G protein in the mediation of the growth arrest. Lack of growth-arresting activity of mammalian βγ complexes (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 12 (1996), S. 41-51 
    Details
    ISSN: 0749-503X
    Keywords: STE4 ; STE18 ; G proteins ; signal transduction ; yeast ; structure-function ; Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Mating pheromone signal transduction in Saccharomyces cerevisiae involves a G protein composed to Scg1p (Gpa1p), Ste4p and Ste18p subunits, homologous to the α, β and γ subunits of mammalian G proteins. Growth arrest in G1 phase is activated by the Ste4p/Ste18p complex via a downstream pathway and it is negatively controlled by the Scg1p subunit. Here we explored whether mammalian β or γ subunits could functionally substitute for their yeast homologues. While no evidence was obtained for functional replacement of Ste4p and Ste18p, we found that overexpression of Ste18p potentiated the effect of hybrid proteins in which the N terminus of the Ste4p subunit was replaced by that of the mammalian β, ste4 mutants having deletions in the N terminus showed a decreased activity in signalling to the downstream effector of the pheromone response. This defect was totally cured by overexpression of Ste18p, indicating that the truncated forms of Ste4p have retained their ability to form an active complex with Ste18p. Removal of six amino acids from the C terminus of Ste4p rendered a completely inactive subunit and this defect persisted in hybrids where the C terminus was placed by that of the β subunit, indicating that the C terminus of Ste4p is essential to trigger the effector of the yeast pheromone response pathway.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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    Paper (German National Licenses)
  • 5
    Electronic Resource
    Electronic Resource
    Isolation of a gene encoding a G protein α subunit involved in the regulation of cAMP levels in the yeast Kluyveromyces lactis (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 12 (1996), S. 1125-1133 
    Details
    ISSN: 0749-503X
    Keywords: G proteins ; α subunit ; signal transduction ; Kluyveromyces lactis ; cAMP ; yeast ; Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Using chromosomal DNA from Kluyveromyces lactis as template and oligodeoxynucleotides designed from conserved regions of various G protein alpha subunits we were able to amplify by the polymerase chain reaction two products of approximately 0·5 kb (P-1) and 0·8 kb (P-2). Sequencing showed that these two fragments share high homology with genes coding for the Gα subunits from different sources. Using the P-1 fragment as a probe we screened a genomic library from K. lactis and we cloned a gene (KlGPA2) whose deduced amino acid sequence showed, depending on the exact alignment, 62% similarity and 38% identity with Gpa1p and 76% similarity and 63% identity with Gpa2p, the G protein α subunits from Saccharomyces cerevisiae. KlGPA2 is a single-copy gene and its disruption rendered viable cells with significantly reduced cAMP level, indicating that this Gα subunit may be involved in regulating the adenylyl cyclase activity, rather than participating in the mating pheromone response pathway. KlGpa2p shares some structural similarities with members of the mammalian Gαs family (stimulatory of adenylyl cyclase) including the absence in its N-terminus of a myristoyl-modification sequence. The sequence reported in this paper has been deposited in the GenBank data base (Accession No. L45105).
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
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    Paper (German National Licenses)
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