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  • 1
    ISSN: 1617-4623
    Keywords: Gβ protein ; Schizosaccharomyces pombe ; Sporulation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract ASchizosaccharomyces pombe homolog of mammalian genes encoding G proteinβ subunits,gpb1 +, was cloned by the polymerase chain reaction using primer pairs that correspond to sequences conserved in several Gβ genes of other species followed by screening of genomic and cDNA libraries. Thegpb1 gene encodes 317 amino acids that show 47% homology with human Gβ 1 and Gβ 2 and 40% homology withSaccharomyces cerevisiae Gβ protein. Disruption of thegpb1 gene indicated that this gene is not required for vegetative cell growth. However,gpb1-disrupted haploid cells mated and sporulated faster than wild-type cells, both in sporulation (MEA) and in complex medium (YE): when examined 23 h after transfer to sporulation medium, 35% ofgpb1-disrupted haploid pairs had undergone conjugation and sporulation, whereas only 3–5% of wild-type haploid pairs had done so. Overexpression of thegpb1 gene suppressed this facilitated conjugation and sporulation phenotype ofgpb1-disrupted cells but did not cause any obvious effect in wild-type cells. Co-disruption of one of the twoS. pombe Gα-subunit genes,gpa2, in thegpb1-disrupted cells did not change the accelerated conjugation and sporulation phenotype of thegpb1 − cells. However, co-disruption of theras1 gene abolished thegpb1 − phenotype. These results suggest that Gpbl is a negative regulator of conjugation and sporulation that apparently works upstream of Ras1 function inS. pombe. The possible relationship of Gpbl to two previously identified, putative Gα proteins ofS. pombe is discussed.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1617-4623
    Keywords: Key words Gβ protein ; Schizosaccharomyces pombe ; Sporulation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A Schizosaccharomyces pombe homolog of mammalian genes encoding G protein β subunits, gpb1 +, was cloned by the polymerase chain reaction using primer pairs that correspond to sequences conserved in several Gβ genes of other species followed by screening of genomic and cDNA libraries. The gpb1 gene encodes 317 amino acids that show 47% homology with human Gβ1 and Gβ2 and 40% homology with Saccharomyces cerevisiae Gβ protein. Disruption of the gpb1 gene indicated that this gene is not required for vegetative cell growth. However, gpb1-disrupted haploid cells mated and sporulated faster than wild-type cells, both in sporulation (MEA) and in complex medium (YE): when examined 23 h after transfer to sporulation medium, 35% of gpb1-disrupted haploid pairs had undergone conjugation and sporulation, whereas only 3–5% of wild-type haploid pairs had done so. Overexpression of the gpb1 gene suppressed this facilitated conjugation and sporulation phenotype of gpb1-disrupted cells but did not cause any obvious effect in wild-type cells. Co-disruption of one of the two S. pombe Gα-subunit genes, gpa2, in the gpb1-disrupted cells did not change the accelerated conjugation and sporulation phenotype of the gpb1 − cells. However, co-disruption of the ras1 gene abolished the gpb1 − phenotype. These results suggest that Gpbl1 is a nebative regulator of conjugation and sporulation that apparantely works upstream of Ras1 function in S. pombe. The possible relationship of Gpb1 to two previously indentified, putative Gα proteins of S. pombe is discussed.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 7 (1991), S. 693-698 
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; protein sorting ; post-translational modification ; allantoin pathway ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The DAL3 gene has been sequenced and found to encode a 195 amino acid protein with a molecular weight of 21 727. The four carboxy-terminal amino acids of DAL3 product (Cys-Ile-Ile-Ile) are homologous to those (CAAX) previously shown to be the primary structural signal for post-translational farnesylation of yeast RAS protein and mating factor. This modification is reported to be responsible for membrane localization of proteins containing it. The upstream region of DAL3 contains six copies of a sequence that is homologous to the positively acting DAL UASNTR reported to be required for transcriptional activation of the DAL5 and DAL7 genes. Missing from the DAL3 upstream region were any sequences related to those shown to be required for a DAL7 response to inducer, the UIS element. This correlates with the previous report that DAL3 expression is independent of the allantoin pathway inducer.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Phospholipase D2 (PLD2) is expressed in brain andinhibited by synuclein, which is involved in Parkinson's and Alzheimer'sdiseases. However, the activation mechanism of PLD2 in neuronal cells has notbeen defined clearly. Hydrogen peroxide (H2O2) playsroles in the neurodegenerative diseases and also acts as a second messenger ofvarious molecules such as nerve growth factor. To study regulation mechanismsof PLD2 by H2O2 in neuronal cells, we have made stablePC12 cell lines expressing PLD2 (PLD2-PC12 cells). H2O2treatment stimulated PLD activity in PLD2-PC12 cells in a dose- andtime-dependent manner. This activation was inhibited by the treatment withprotein kinase C (PKC) inhibitors or by depletion of PKCα, -δ, and-ε. Phorbol ester markedly activated PLD2. Co-treatment with phorbolester and H2O2 did not show an additive effect.Chelation of extracellular calcium substantially blocked theH2O2-induced activation of PLD2. A calcium ionophoreinduced PLD2 activation in a PKC-dependent manner. Protein-tyrosine kinaseinhibitors inhibited H2O2-induced PLD activationslightly. These data indicate that H2O2 can activatePLD2 in PC12 cells and that this activation is largely dependent on PKC andCa2+ ions and minimally dependent on tyrosine phosphorylation.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 8 (1992), S. 997-1006 
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; Permeases ; transport ; allantoin ; uracil ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We have determined the structure of the allantoin permease (DAL4) gene of Saccharomyces cerevisiae. The gene patatively encodes a hydrophobic protein with a Mr of 71 755. It possesses the alternating hydrophobic-hydrophilic regions similar to those found in many other integral membrane proteins. The most striking feature of the allantoin permease component encoded by DAL4 is its striking similarity to the uracil permease component encoded by FUR4 Although data available indicate that these proteins do not share any overlap of function, their predicted protein sequences are 68% identical, 81% similar, and their DNA sequences are 70% identical. The upstream regulatory region of DAL4 contains all lof the characterized cis-acting elements previously reported for inducible allantoin pathway genes: six sequences homologous to UAS NTR, the element responsible for nitrogen catabolite repression-sensitive activation of allantoin pathway gene expression, and two sequences homologous to the cis-acting element responsible for inducere-responsiveness of the allantoin pathway genes, UIS. The finding of these homologous sequences predicted to exist on the basis of DAL4's expression characteristics, supports and strengthens the suggestion that these elements mediate the functions we have we have previously ascribed to them.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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