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  • Caffeine  (2)
  • Lycopersicon esculentum
  • Springer  (3)
  • American Chemical Society
  • 1995-1999  (3)
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  • Springer  (3)
  • American Chemical Society
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Year
  • 1
    Electronic Resource
    Electronic Resource
    Molecular and functional characterization of a mutant allele of the mitogen-activated protein-kinase geneSLT2(MPK1) rescued from yeast autolytic mutants (1996)
    Springer
    Current genetics 29 (1996), S. 516-522 
    Details
    ISSN: 1432-0983
    Keywords: Yeast ; SLT2 ; MAP-kinase ; Caffeine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We have further characterized the functionality of theSaccharomyces cerevisiae geneSLT2(MPK1), coding for a MAP-kinase homolog essential for cell integrity, which is involved in the Pkc1p signalling pathway. This gene was isolated on the basis of its capacity to complement the thermosensitive-autolytic, osmotic-remediable phenotype oflyt2 mutants. Bothslt2A andlyt2 mutants displayed a caffeine-sensitive phenotype consisting of cell lysis that was not dependent on temperature. Caffeine concentrations affecting the growth of these mutant strains were dependent on the genetic background, theSSD1 allele being very significant in this regard. TheSLT2 allele of severallyt2 strains was both rescued and amplified by PCR. The recovered allele was shown to be non-functional as it could not complement the lytic phenotype of both deletion (slt2Δ) andlyt2 strains. After nucleotide sequencing of the recovered allele, we found that the defect oflyt2 mutants consists in a substitution of an aspartic acid for a glycine at position 35 of the amino-acid sequence of Slt2p. Gly35 is the third glycine of a glycine cluster (Gly-X-Gly-X-X-Gly), a conserved region in protein kinases and other nucleotide-binding proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02426955
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  • 2
    Electronic Resource
    Electronic Resource
    Molecular and functional characterization of a mutant allele of the mitogen-activated protein-kinase gene SLT2(MPK1) rescued from yeast autolytic mutants (1996)
    Springer
    Current genetics 29 (1996), S. 516-522 
    Details
    ISSN: 1432-0983
    Keywords: Keywords Yeast ; SLT2 ; MAP-kinase ; Caffeine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract  We have further characterized the functionality of the Saccharomyces cerevisiae gene SLT2(MPK1), coding for a MAP-kinase homolog essential for cell integrity, which is involved in the Pkc1p signalling pathway. This gene was isolated on the basis of its capacity to complement the thermosensitive-autolytic, osmotic-remediable phenotype of lyt2 mutants. Both slt2Δ and lyt2 mutants displayed a caffeine-sensitive phenotype consisting of cell lysis that was not dependent on temperature. Caffeine concentrations affecting the growth of these mutant strains were dependent on the genetic background, the SSD1 allele being very significant in this regard. The SLT2 allele of several lyt2 strains was both rescued and amplified by PCR. The recovered allele was shown to be non-functional as it could not complement the lytic phenotype of both deletion (slt2Δ) and lyt2 strains. After nucleotide sequencing of the recovered allele, we found that the defect of lyt2 mutants consists in a substitution of an aspartic acid for a glycine at position 35 of the amino-acid sequence of Slt2p. Gly35 is the third glycine of a glycine cluster (Gly-X-Gly-X-X-Gly), a conserved region in protein kinases and other nucleotide-binding proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002940050080
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Molecular characterization of glyoxalase-I from a higher plant; upregulation by stress (1995)
    Springer
    Plant molecular biology 29 (1995), S. 1223-1233 
    Details
    ISSN: 1573-5028
    Keywords: expression pattern ; glyoxalase-I ; Lycopersicon esculentum ; phloem ; sequence ; salt-stress
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A cDNA, GLX1, encoding glyoxalase-I was isolated by differential screening of salt-induced genes in tomato. Glyoxalases-I and-II are ubiquitous enzymes whose functions are not clearly understood. They may serve to detoxify methylglyoxal produced from triosephosphates in all cells. The protein encoded by GLX1 shared 49.4% and 58.5% identity with glyoxalase-I isolated from bacteria and human, respectively. Furthermore, yeast cells expressing GLX1 showed a glyoxalase-I specific activity 20-fold higher than non-transformed cells. Both GLX1 mRNA and glyoxalase-I polypeptide levels increased 2- to 3-fold in roots, stems and leaves of plants treated with either NaCl, mannitol, or abscisic acid. Immunohistochemical localization indicated that glyoxalase-I was expressed in all cell types, with preferential accumulation in phloem sieve elements. This expression pattern was not appreciably altered by salt-stress. We suggest that the increased expression of glyoxalase-I may be linked to a higher demand for ATP generation and to enhanced glycolysis in salt-stressed plants.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00020464
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