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  • 1
    Electronic Resource
    Electronic Resource
    Genetic analyses of yeast protein serine/threonine phosphatases (1994)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 117 (1994), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Protein phosphorylation is an important regulatory phenomenon in yeasts just as in other eukaryotic cells and controls a wide variety of cellular processes. The importance of protein phosphatases as well as protein kinases as key elements in such control is becoming increasingly clear. Over the past four years since the first yeast protein phosphatase gene was isolated, many more such genes have been described and the number of genes encoding protein phosphatase catalytic subunits in Saccharomyces cerevisiae has comfortably entered double figures. Given the genetic approaches available, yeasts offer powerful systems for addressing the cellular roles of these enzymes. This review summarises the results of genetic studies aimed at determining the functions of protein serine/threoninc phosphatases in yeast.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1994.tb06753.x
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  • 2
    Electronic Resource
    Electronic Resource
    Kluyveromyces lactis zymocin mode of action is linked to RNA polymerase II function via Elongator (2001)
    Oxford, UK : Blackwell Science Ltd
    Molecular microbiology 42 (2001), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The putative Kluyveromyces lactis zymocin target complex, TOT, from Saccharomyces cerevisiae comprises five Tot proteins, four of which are RNA polymerase II (RNAP II) Elongator subunits. Recently, two more Elongator subunit genes, ELP6 (TOT6) and ELP4 (TOT7), have been identified. Deletions of both TOT6 and TOT7 result in the complex tot phenotype, including resistance to zymocin, thermosensitivity, slow growth and hypersensitivity towards drugs, thus reinforcing the notion that TOT/Elongator may be crucial in signalling zymocicity. Mutagenesis of ELP3/TOT3, the Elongator histone acetyltransferase (HAT) gene, revealed that zymocin sensitivity could be uncoupled from Elongator wild-type function, indicating that TOT interacts genetically with zymocin. To test the possibility that zymocin functions by affecting RNAP II activity in a TOT/Elongator-dependent manner, global poly(A)+ mRNA levels were found to decline drastically on zymocin treatment. Moreover, cells overexpressing Fcp1p, the RNAP II carboxy-terminal domain phosphatase, acquired partial zymocin resistance, whereas cells underproducing RNAP II became zymocin hypersensitive. This suggests that zymocin may convert TOT/Elongator into a cellular poison toxic for RNAP II function and eventually leading to the observed G1 cell cycle arrest.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.2001.02705.x
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  • 3
    Electronic Resource
    Electronic Resource
    Global analysis of protein phosphorylation in yeast (2005)
    [s.l.] : Nature Publishing Group
    Nature 438 (2005), S. 679-684 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Protein phosphorylation is estimated to affect 30% of the proteome and is a major regulatory mechanism that controls many basic cellular processes. Until recently, our biochemical understanding of protein phosphorylation on a global scale has been extremely limited; only one half of the yeast ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nature04187
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  • 4
    Electronic Resource
    Electronic Resource
    Protein interactions within Saccharomyces cerevisiae Elongator, a complex essential for Kluyveromyces lactis zymocicity (2002)
    Oxford, UK : Blackwell Science Ltd
    Molecular microbiology 45 (2002), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: mTn3-tagging identified Kluyveromyces lactis zymocin target genes from Saccharomyces cerevisiae as TOT1–3/ELP1–3 coding for the RNA polymerase II (pol II) Elongator histone acetyltransferase (HAT) complex. tot phenotypes resulting from mTn3 tagging were similar to totΔ null alleles, suggesting loss of Elongator's integrity. Consistently, the Tot1–3/Elp1–3 proteins expressed from the mTn3-tagged genes were all predicted to be C-terminally truncated, lacking ≈ 80% of Tot1p, five WD40 Tot2p repeats and two HAT motifs of Tot3p. Besides its role as a HAT, Tot3p assists subunit communication within Elongator by mediating Tot2–Tot4, Tot2–Tot5, Tot2–Tot1 and Tot4–Tot5 protein–protein interactions. TOT1 and TOT2 are essential for Tot4–Tot2 and Tot4–Tot3 interactions respectively. The latter was lost with a C-terminal Tot2p truncation; the former was affected by progressively truncating TOT1. Despite being dispensable for Tot4–Tot2 interaction, the extreme C-terminus of Tot1p may play a role in TOT/Elongator function, as its truncation confers zymocin resistance. Tot4p/Kti12p, an Elongator-associated factor, also interacted with pol II and could be immunoprecipitated while being bound to the ADH1 promoter. Two-hybrid analysis showed that Tot4p also interacts with Cdc19p, suggesting that Tot4p plays an additional role in concert with Cdc19p, perhaps co-ordinating cell growth with carbon source metabolism.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.2002.03055.x
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  • 5
    Electronic Resource
    Electronic Resource
    Elongator's toxin-target (TOT) function is nuclear localization sequence dependent and suppressed by post-translational modification (2003)
    Oxford, UK : Blackwell Science Ltd
    Molecular microbiology 49 (2003), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The toxin target (TOT) function of the Saccharomyces cerevisiae Elongator complex enables Kluyveromyces lactis zymocin to induce a G1 cell cycle arrest. Loss of a ubiquitin-related system (URM1–UBA4 ) and KTI11 enhances post-translational modification/proteolysis of Elongator subunit Tot1p (Elp1p) and abrogates its TOT function. Using TAP tagging, Kti11p contacts Elongator and translational proteins (Rps7Ap, Rps19Ap Eft2p, Yil103wp, Dph2p). Loss of YIL103w and DPH2 (involved in diphtheria toxicity) suppresses zymocicity implying that both toxins overlap in a manner mediated by Kti11p. Among the pool that co-fractionates with RNA polymerase II (pol II) and nucleolin, Nop1p, unmodified Tot1p dominates. Thus, modification/proteolysis may affect association of Elongator with pol II or its localization. Consistently, an Elongator-nuclear localization sequence (NLS) targets green fluorescent protein (GFP) to the nucleus, and its truncation yields TOT deficiency. Similarly, KAP120 deletion rescues cells from zymocin, suggesting that Elongator's TOT function requires NLS- and karyopherin-dependent nuclear import.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.2003.03632.x
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  • 6
    Electronic Resource
    Electronic Resource
    Protein A–calmodulin fusions: a novel approach for investigating calmodulin function in yeast (1992)
    Oxford, UK : Blackwell Publishing Ltd
    Molecular microbiology 6 (1992), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: A novel gene fusion approach which may be of more general use has been developed for investigating the function of calmodulin in the budding yeast Saccharomyces cerevisiae. By fusing a portion of the Staphylococcus aureus spa gene (encoding protein A) to CMD1, the S. cerevisiae gene encoding calmodulin, we have generated a yeast calmodulin with an affinity tag able to bind immunoglobulins. The chimaeric protein A–calmodulin (ProtA–CaM) polypeptide functions in vivo and shows Ca2+-dependent binding to calmodulin target proteins. The spa–CMD1 fusion has been used (i) to prepare (by affinity chromatography) a fraction of yeast proteins which interact with calmodulin, (ii) to isolate genes encoding calmodulin target proteins by direct screening of an expression library, and (iii) to visualize calmodulin-binding proteins in crude extracts by Western blot analysis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.1992.tb01519.x
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  • 7
    Electronic Resource
    Electronic Resource
    Adaptive generation of surfaces in volume data (1993)
    Springer
    The visual computer 9 (1993), S. 182-199 
    Details
    ISSN: 1432-2315
    Keywords: Volume visualization ; Marching cubes ; Adaptive subdivision ; Generic surfaces
    Source: Springer Online Journal Archives 1860-2000
    Topics: Computer Science
    Notes: Abstract A widespread approach to generating polygonal approximations of iso-surfaces or contour surfaces in volume data is the socalled marching-cubes algorithm. This algorithm, however, has the disadvantage that the number of polygonal chains generated is considerable. The splitting-box algorithm presented here reduces the number of polygonal chains by adapting their size to the shape of the surface. The resulting polygonal chains offer a wide spectrum for representing the contour surface. An exact representation is achieved by a new type of generic patches calculated from the polygonal chains. Approximations of different quality may be obtained by combining the algorithm generating the patches with simple triangulations.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01901723
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  • 8
    Electronic Resource
    Electronic Resource
    Toxin arrest (1990)
    [s.l.] : Nature Publishing Group
    Nature 346 (1990), S. 518-518 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] SIR-Bradshaw in Scientific Correspondence1 has suggested the interesting idea that the Kluyveromyces lactis toxin may arrest the growth of sensitive yeast cells by interfering with cell-wall biosynthesis. The hypothesis is based on the observation that a region of the largest (a) subunit of the ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/346518b0
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  • 9
    Electronic Resource
    Electronic Resource
    Kluyveromyces lactis toxin does not inhibit yeast adenylyl cyclase (1989)
    [s.l.] : Nature Publishing Group
    Nature 341 (1989), S. 666-668 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The addition of toxin to a culture of sensitive 5. cerevisiae cells leads to a cessation of cell division within 1-2 generations, as indicated by the complete block in accumulation of cells after treatment with toxin (Fig. la). In treated cultures, we saw no further increase in cell numbers for ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/341666a0
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  • 10
    Electronic Resource
    Electronic Resource
    A novel `two-component' protein containing histidine kinase and response regulator domains required for sporulation in Aspergillus nidulans (2000)
    Springer
    Current genetics 37 (2000), S. 364-372 
    Details
    ISSN: 1432-0983
    Keywords: Key wordsAspergillus nidulans ; tcsA gene ; Two-component system
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We have characterised a novel Aspergillus nidulans gene encoding a `two-component' signalling protein (tcsA). tcsA encodes both a histidine kinase domain and a response regulator domain similar to those found in bacterial, lower eukaryotic and plant members of the two-component family of proteins, while two PAS domains in the amino-terminal region of the predicted tcsA product may monitor the signal which regulates a tcsA histidine kinase-response regulator phosphorelay. While tcsA is nonessential for vegetative growth, cells lacking the gene are unable to produce conidia on standard Aspergillus growth media. However, tcsA is not absolutely required for production since this defect is suppressed by growth on 1 M sorbitol.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002940000123
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