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  • 1
    Digitale Medien
    Digitale Medien
    College Park, Md. : American Institute of Physics (AIP)
    The Journal of Chemical Physics 110 (1999), S. 1154-1162 
    ISSN: 1089-7690
    Quelle: AIP Digital Archive
    Thema: Physik , Chemie und Pharmazie
    Notizen: The kinetics of adsorption and abstraction for the system H(D) on Al(111) and Ni(111) has been investigated using an efficient atomic beam source, thermal desorption spectroscopy, and multiplexed mass spectrometry. The initial sticking coefficient of atomic hydrogen on Ni(111) is 1.0 and independent of the angle of incidence. For H on Al(111) the initial sticking coefficient is 0.6 and increases with increasing angle of incidence (S(cursive-phi)∼cos−0.4 cursive-phi). On Al(111) preadsorbed oxygen leads to a decrease of the initial sticking coefficient for H down to 0.1; potassium on the other hand has no significant influence on the initial sticking probability. On both surfaces, Ni(111) and Al(111), abstraction of deuterium proceeds at a surface temperature of 150 K due to impinging H atoms (H+D→HD), with an initial abstraction coefficient of 0.20 on Al(111) and 0.12 on Ni(111). In the case of Al(111) this coefficient is nearly independent of the initial D coverage and therefore the abstraction reaction cannot be described by a simple Eley–Rideal process, but rather by a hot-precursor mechanism. In addition to abstraction there is also a small probability for the removal of an adsorbed species by a collision induced desorption process. Abstraction of deuterium by impinging H-atoms is strongly affected by modification of the Al(111) surface, either by oxygen or by potassium. Oxygen decreases the HD abstraction coefficient, probably by inhibiting the hot-precursor state of H on the surface. Potassium increases the HD abstraction rate, most likely by increasing the lifetime of atomic hydrogen in the precursor state. © 1999 American Institute of Physics.
    Materialart: Digitale Medien
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  • 2
    Digitale Medien
    Digitale Medien
    Springer
    Applied physics 67 (1998), S. 637-644 
    ISSN: 1432-0630
    Schlagwort(e): PACS: 68.10.Jy; 68.45.Da; 82.65.Pa
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Maschinenbau , Physik
    Materialart: Digitale Medien
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  • 3
    ISSN: 1432-0983
    Schlagwort(e): Key wordsSKP1 ; CTF13 ; Kinetochore ; Cell cycle ; Kluyveromyces lactis
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract The SKP1 gene of Kluyveromyces lactis was isolated as a suppressor of a lethal temperature-sensitive mutation in the Saccharomyces cerevisiae CTF13 gene (Chromosome Transmission Factor 13). KlSKP1 was localized at chromosome V, adjacent to KlPAS3. A similar arrangement of the two genes is present in S. cerevisiae. Disruption of the KlSKP1 gene was lethal, whereas overexpression of KlSKP1 lead to a decreased growth rate, to swollen and chain-forming cells with an increased DNA content, and to decreased plasmid stability. In both yeasts, promoter constructs lacking most of the purported binding sequence showed increased transcription levels of KlSKP1 in comparison to constructs with the entire promoter.
    Materialart: Digitale Medien
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  • 4
    ISSN: 1432-0983
    Schlagwort(e): Key words Kluyveromyces lactis ; CBF2 ; UBP2 ; Ubiquitination
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract  The Kluyveromyces lactis UBP2 gene was isolated as a suppressor of a temperature-sensitive mutation in CBF2, a gene coding for a centromere-binding protein of Saccharomyces cerevisiae. The UBP genes are hydrolases than can cleave a ubiquitin moiety from a protein substrate. KlUBP2 is not essential for growth since a disruption of the KlUBP2 gene had little effect, except for a slight decrease in the growth rate. The stability of centromere-containing plasmids was not influenced either. In addition to KlUBP2, five S. cerevisiae genes involved in the ubiquitination pathway could suppress the ts-mutation in the CBF2 gene, namely UBA1, UBA2, UBP1, UBP2 and YUH1, although YUH1 was the only one that could do this like KlUBP2 from a single-copy plasmid. Surprisingly, these genes encode proteins with antagonistic activity as two, UBA1 and UBA2, are ubiquitin-activating enzymes whereas the other three are de-ubiquitinating hydrolases.
    Materialart: Digitale Medien
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  • 5
    ISSN: 1617-4623
    Schlagwort(e): Key wordsAgrobacterium tumefaciens ; Kluyveromyces lactis ; Gene targeting ; Recombination
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract The soil bacterium Agrobacterium tumefaciens can transfer a part of its tumour-inducing (Ti) plasmid, the T-DNA, to plant cells. The virulence (vir) genes, also located on the Ti plasmid, encode proteins involved in the transport of T-DNA into the plant cell. Once in the plant nucleus, T-DNA is able to integrate into the plant genome by an illegitimate recombination mechanism. The host range of A. tumefaciens is not restricted to plant species. A. tumefaciens is also able to transfer T-DNA to the yeast Saccharomyces cerevisiae. In this paper we demonstrate transfer of T-DNA from A. tumefaciens to the yeast Kluyveromyces lactis. Furthermore, we found that T-DNA serves as an ideal substrate for gene targeting in K. lactis. We have studied the efficiency of gene targeting at the K. lactis TRP1 locus using either direct DNA transfer (electroporation) or T-DNA transfer from Agrobacterium. We found that gene targeting using T-DNA was at least ten times more efficient than using linear double-stranded DNA introduced by electroporation. Therefore, the outcome of gene targeting experiments in some organisms may depend strongly upon the DNA substrate used.
    Materialart: Digitale Medien
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  • 6
    ISSN: 0749-503X
    Schlagwort(e): Kluyveromyces lactis ; CBF5 ; centromere ; nucleolus ; Life and Medical Sciences ; Genetics
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Biologie
    Notizen: The gene coding for the centromere-binding factor 5 (CBF5) of Kluyveromyces lactis has been isolated by hybridization of a Saccharomyces cerevisiae CBF5 DNA probe to a K. lactis library. The amino acid sequence of KlCbf5 is highly homologous, 88% identity, to ScCbf5, but also to the rat protein Nap57 (64% identity). The main difference between both yeast proteins and the rat protein is the presence of a lysine-rich domain with KKE/D repeats in the C-terminal part of the protein. These repeats are thought to be involved in binding of the protein to microtubules. Deletion of the KKE/D domain in KlCbf5 however, has no discernible effect on growth on rich medium, sensitivity to the microtubule-destabilizing drug benomyl or segregation of a reporter plasmid. On the other hand, insertion of two leucine residues adjacent to the KKE domain increases the loss rate of a reporter plasmid. In both yeasts complementation of a lethal CBF5 disruption with the heterologous gene results in a slight increase in benomyl sensitivity. A possible role of CBF5 in chromosome segregation will be discussed. © 1998 John Wiley & Sons, Ltd.
    Zusätzliches Material: 5 Ill.
    Materialart: Digitale Medien
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