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  • 1
    Electronic Resource
    Electronic Resource
    Ultrastructural localization of nucleic acid sequences in Saccharomyces cerevisiae nucleoli (1991)
    Springer
    Chromosoma 100 (1991), S. 519-523 
    Details
    ISSN: 1432-0886
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The putative nucleolus in Saccharomyces cerevisiae is visible in electron micrographs as a darkly stained, crescent-shaped structure associated with the nuclear envelope. The haploid yeast genome contains 100 200 tandem copies of a 9.1 kb ribosomal DNA (rDNA) repeat predicted to reside in this structure. We combined in situ hybridization of non-isotopically labeled probes to isolated S. cerevisiae nuclei with immunogold detection to localize rDNA and rRNA precursor sequences in nuclei at the electron microscope (EM) level. Gold particles are restricted to defined regions of nuclei which appear more electron dense than the bulk of the nucleus and which generally exhibit the crescent shape typical of the structure thought to be the nucleolus. In addition, snR17, the yeast homolog of mammalian U3, a nucleolar-restricted small nuclear RNA (snRNA), was localized to the same electron dense region of the nucleus. These data, in conjunction with published immunofluorescent localizations of nucleolarassociated antigens, provide definitive proof that the dense crescent is the nucleolus. Finally, the technique described is applicable to probing nuclear organization in a genetically manipulable system.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00352202
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  • 2
    Electronic Resource
    Electronic Resource
    A yeast mutant, PRP20, altered in mRNA metabolism and maintenance of the nuclear structure, is defective in a gene homologous to the human gene RCC1 which is involved in the control of chromosome condensation (1990)
    Springer
    Molecular genetics and genomics 224 (1990), S. 72-80 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Splicing ; Nuclear structure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary We report on the characterization of the yeast prp20-1 mutant. In this temperature-sensitive mutant, multiple steps of mRNA metabolism are affected. The prp20-1 mutant strain showed alterations in mRNA steady-state levels, defective mRNA splicing and changes in transcription initiation or termination when shifted from the permissive to the non-permissive temperature. In addition, a change in the structure of the nucleus in these cells became apparent. Electron microscopy revealed an altered structure of the nucleoplasm of prp20-1 mutant cells when grown at the no-permissive temperature that was not observed in cells grown at the permissive temperature or in wild-type cells. The wild-type PRP20 gene was isolated and sequenced. The putative PRP20 protein has a molecular weight of 52 kDa. We found that the PRP20 gene is identical to the yeast SRM1 gene (Clark and Sprague 1989). In addition, the PRP20 protein sequence shows significant sequence similarity to the human RCC1 protein (Ohtsubo et al. 1987). This protein has been implicated in the control of chromosome condensation. Based on the phenotype of the prp20-1 mutant and the observed sequence similarity to the human RCC1 protein, we postulate that the yeast PRP20 protein is involved in the control of nuclear organization.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00259453
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  • 3
    Electronic Resource
    Electronic Resource
    Site-directed mutagenesis of the yeast PRP20/1SRM1 gene reveals distinct activity domains in the protein product (1994)
    Springer
    Molecular genetics and genomics 245 (1994), S. 32-44 
    Details
    ISSN: 1617-4623
    Keywords: RCC1 ; PRP20/SRM1 ; Double-stranded ; DNA binding
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Prp20/Srm1, a homolog of the mammalian protein RCC1 in Saccharomyces cerevisiae, binds to double-stranded DNA (dsDNA) through a multicomponent complex in vitro. This dsDNA-binding capability of the Prp20 complex has been shown to be cell-cycle dependent; affinity for dsDNA is lost during DNA replication. By analyzing a number of temperature sensitive (ts) prp20 alleles produced in vivo and in vitro, as well as site-directed mutations in highly conserved positions in the imperfect repeats that make up the protein, we have determined a relationship between the residues at these positions, cell viability, and the dsDNA-binding abilities of the Prp20 complex. These data reveal that the essential residues for Prp20 function are located mainly in the second and the third repeats at the amino-terminus and the last two repeats, the seventh and eighth, at the carboxyl-terminus of Prp20. Carboxyl-terminal mutations in Prp20 differ from amino-terminal mutations in showing loss of dsDNA binding: their conditional lethal phenotype and the loss of dsDNA binding affinity are both suppressible by overproduction of Gsp1, a GTP-binding constituent of the Prp20 complex, homologous to the mammalian protein TC4/Ran. Although wild-type Prp20 does not bind to dsDNA on its own, two mutations in conserved residues were found that caused the isolated protein to bind dsDNA. These data imply that, in situ, the other components of the Prp20 complex regulate the conformation of Prp20 and thus its affinity for dsDNA. Gsp1 not only influences the dsDNA-binding ability of Prp20 but it also regulates other essential function(s) of the Prp20 complex. Overproduction of Gsp1 also suppresses the lethality of two conditional mutations in the penultimate carboxyl-terminal repeat of Prp20, even though these mutations do not eliminate the dsDNA binding activity of the Prp20 complex. Other site-directed mutants reveal that internal and carboxyl-terminal regions of Prp20 that lack homology to RCC1 are dispensable for dsDNA binding and growth.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00279748
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  • 4
    Electronic Resource
    Electronic Resource
    Analysis of yeast prp20 mutations and functional complementation by the human homologue RCC1, a protein involved in the control of chromosome condensation (1991)
    Springer
    Molecular genetics and genomics 227 (1991), S. 417-423 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; mRNA metabolism ; Nucleus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Mutations in the PRP20 gene of yeast show a pleiotropic phenotype, in which both mRNA metabolism and nuclear structure are affected. srm1 mutants, defective in the same gene, influence the signal transduction pathway for the pheromone response. The yeast PRP20/SRM1 protein is highly homologous to the RCC1 protein of man, hamster and frog. In mammalian cells, this protein is a negative regulator for initiation of chromosome condensation. We report the analysis of two, independently isolated, recessive temperature-sensitive prp20 mutants. They have identical G to A transitions, leading to the alteration of a highly conserved glycine residue to glutamic acid. By immunofluorescence microscopy the PRP20 protein was localized in the nucleus. Expression of the RCC1 protein can complement the temperature-sensitive phenotype of prp20 mutants, demonstrating the functional similarity of the yeast and mammalian proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00273932
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  • 5
    Electronic Resource
    Electronic Resource
    Evaporation rates of volatile liquids in a laminar flow system: Part II. Liquid mixtures (1970)
    Hoboken, NJ : Wiley-Blackwell
    AIChE Journal 16 (1970), S. 69-75 
    Details
    ISSN: 0001-1541
    Keywords: Chemistry ; Chemical Engineering
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: An approach has been developed for predicting rates of interphase mass transfer under conditions of high flux and high concentration level. A rectangular channel device has been used to measure rates of evaporation of four solutes, carbon disulfide, n-pentane, cyclopentane, and ethyl ether, from n-tridecane into flowing nitrogen. The evaporation rate of carbon disulfide agreed with the prediction of the interphase theory up to a carbon disulfide mole fraction of 0.30 in the bulk liquid. For the other three systems, a concentration gradient induced, surface tension driven cellular convection served to increase liquid-phase coefficients substantially. A correlation was obtained for the effect of this cellular motion on the liquid-phase mass transfer coefficient.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/aic.690160115
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  • 6
    Electronic Resource
    Electronic Resource
    Evaporation rates of volatile liquids in a laminar flow system: Part I. Pure liquids (1970)
    Hoboken, NJ : Wiley-Blackwell
    AIChE Journal 16 (1970), S. 64-69 
    Details
    ISSN: 0001-1541
    Keywords: Chemistry ; Chemical Engineering
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Normal pentane and isopentane were evaporated into nitrogen in laminar, concurrent flow in a rectangular channel. Composition profiles within the gas phase were measured, and the evaporation rates were compared with theoretical predictions with satisfactory agreement. The interfacial mole fraction of the evaporating species in the gas phase ranged as high as 0.74. A solution is reported for the Leveque problem under high flux conditions.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/aic.690160114
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  • 7
    Electronic Resource
    Electronic Resource
    Incipient vortex formation in baffled agitated vessels (1964)
    Hoboken, NJ : Wiley-Blackwell
    AIChE Journal 10 (1964), S. 420-422 
    Details
    ISSN: 0001-1541
    Keywords: Chemistry ; Chemical Engineering
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/aic.690100331
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  • 8
    Electronic Resource
    Electronic Resource
    Identification of a Saccharomyces cerevisiae homolog of the SNF2 transcrioptional regulator in the DNA sequence of an 8·6 kb region in the LTE1-CYS1 interval on the left arm of chormosome I (1992)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 8 (1992), S. 133-145 
    Details
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; Chromosome I ; sequence ; transcriptional regulators ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The DNA sequence of an 8·6 kb region of the left arm of chromosome I has been determined. This region, between the LTEL and CYS1 loci, is approximately 40 kb from centromere. There are six potential open-reading frames (ORFs), Provisionally nemed YAL001-006 within this fragment of chromosome I. Four of these ORFs can be aligned with Previously indentified FUN transcripts: FUN28 with YAL006, FUN29 with YAL004, FUN30 with YAL001 and FUN31 with YAL002. The YAL001 ORF shows significant homology to the SNF2 transcriptional regulator. A region of the DNA contains an extensive repeat of the bases C-A-T positioned in the 5′ terminus of the YAL004 promoter region.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320080208
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  • 9
    Electronic Resource
    Electronic Resource
    The yal017 gene on the left arm of chromosome I of Saccharomyces cerevisiae encodes a putative serine/threonine protein kinase (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 543-549 
    Details
    ISSN: 0749-503X
    Keywords: Protein kinase ; yeast chromosome I ; genome sequencing ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The DNA sequence of a region between the LTE1 and CYS3 genes on the left arm of chromosome I from Saccharomyces cerevisiae contains an open reading frame (ORF), YAL017, corresponding to the 5·0 kb FUN31 (Function Unknown Now) transcribed region. The predicted protein from this ORF contains 1358 amino acid residues with a molecular weight of 152 531, and an identifiable serine/threonine protein kinase catalytic domain. When compared with other yeast protein kinases, the Ya1017p kinase most resembles the SNF1 serine/threonine protein kinase which is involved in regulating sucrose fermentation genes. The Ya1017p kinase shows highest amino acid identities with two mammalian carcinoma-related serine/threonine protein kinases; PIM-1, which shows induced expression in T-cell lymphomas; and p78A1, whose expression is lost in human pancreatic carcinomas. Gene disruption of YAL017 indicates that it is non-essential for growth on glucose.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090511
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  • 10
    Electronic Resource
    Electronic Resource
    I. Yeast sequencing reports. LTE1 of Saccharomyces cerevisiae is a 1435 codon open reading frame that has sequence similarities to guanine nucleotide releasing factors (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 10 (1994), S. 953-958 
    Details
    ISSN: 0749-503X
    Keywords: Low temperature sensitivity ; CDC25 ; SDC25 ; BUD5 ; STE6 ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The DNA sequence of the LTE1 gene on the left arm of chromosome I of Saccharomyces cerevisiae has been determined. The LTE1 open reading frame comprises 4305 bp that can be translated into 1435 amino acid residues. The position of this open reading frame corresponds well to that of a 4·7 kb transcript that has been mapped to this position. The derived amino acid sequence has significant similarities to the amino acid sequence of the guanine nucleotide releasing factor isolated from a rat brain library. The carboxy-terminus of the LTE1 protein also shows similarities to other guanine nucleotide exchange factors of the S. cerevisiae CDC25 family. The sequence has been deposited in the GenBank data library under Accession Number L20125.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320100710
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