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  • 1
    Electronic Resource
    Electronic Resource
    Yeast chitin synthases 1 and 2 consist of a non-homologous and dispensable N-terminal region and of a homologous moiety essential for function (1996)
    Springer
    Molecular genetics and genomics 252 (1996), S. 420-428 
    Details
    ISSN: 1617-4623
    Keywords: Key words Saccharomyces cerevisiae ; Chitin synthases ; Septum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract  Predicted protein sequences of fungal chitin synthases can be divided into a non-homologous N-terminal region and a C-terminal region that shows significant homology among the various synthases. We have explored the function of these domains by constructing a series of nested deletions, extending from either end, in the CHS1 and CHS2 genes of Saccharomyces cerevisiae. In both cases, most or all of the sequences encoding the non-homologous N-terminal region (one-third of the protein for Chs1p and about one-fourth for Chs2p) could be excised, with little effect on the enzymatic activity in vitro of the corresponding synthase or on its function in vivo. However, further small deletions (20–25 amino acids) into the homologous region were deleterious to enzymatic activity and function, and often led to changes in the zymogenic character of the enzymes. Similarly, relatively small (about 75 amino acids) deletions from the C-terminus resulted in loss of enzymatic activity and function of both synthases. Thus, it appears that all the information necessary for membrane localization, enzymatic activity and function resides in the homologous regions of Chs1p and Chs2p, a situation that may also apply to other chitin synthases.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02173007
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Yeast chitin synthases 1 and 2 consist of a non-homologous and dispensable N-terminal region and of a homologous moiety essential for function (1996)
    Springer
    Molecular genetics and genomics 252 (1996), S. 420-428 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Chitin synthases ; Septum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Predicted protein sequences of fungal chitin synthases can be divided into a non-homologous N-terminal region and a C-terminal region that shows significant homology among the various synthases. We have explored the function of these domains by constructing a series of nested deletions, extending from either end, in theCHS1 andCHS2 genes ofSaccharomyces cerevisiae. In both cases, most or all of the sequences encoding the non-homologous N-terminal region (one-third of the protein for Chs1p and about one-fourth for Chs2p) could be excised, with little effect on the enzymatic activity in vitro of the corresponding synthase or on its function in vivo. However, further small deletions (20–25 amino acids) into the homologous region were deleterious to enzymatic activity and function, and often led to changes in the zymogenic character of the enzymes. Similarly, relatively small (about 75 amino acids) deletions from the C-terminus resulted in loss of enzymatic activity and function of both synthases. Thus, it appears that all the information necessary for membrane localization, enzymatic activity and function resides in the homologous regions of Chs1p and Chs2p, a situation that may also apply to other chitin synthases.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02173007
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Physiology of acute silver toxicity in the starry flounder (Platichthys stellatus) in seawater (1999)
    Springer
    Journal of comparative physiology 169 (1999), S. 461-573 
    Details
    ISSN: 1432-136X
    Keywords: Key words Ag ; Osmoregulation ; Ionoregulation ; Marine ; Fish
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Physiological effects of exposure to silver (AgCln n−1; 250 μg Ag l−1 or 1000 μg Ag l−1) in seawater fish were investigated using adult starry flounders. While all fish survived up to 10 days in 250 μg Ag l−1, flounders started to die after day 4 in 1000 μg l−1. Dose-dependent increases in plasma and hepatic silver concentrations showed that silver was available for uptake. There were minimal negative effects on hematological parameters, acid-base status, and blood gases. Plasma ammonia showed a pronounced (three- to four-fold), but transient increase in flounders exposed to either 250 μg Ag l−1 or 1000 μg Ag l−1. Whole body ammonia and acid equivalent efflux measurements indicated that ammonia retention was due to a combination of stimulated production and inhibited excretion. In the 1000-μg Ag l−1 group there was a similar transient increase in plasma [magnesium], which was restored by day 4. In contrast, plasma chloride and sodium levels increased gradually towards the point when fish began to die. At 250 μg Ag l−1, the Na+/K+-ATPase activity of the intestine was unaffected but there was a two-fold increase in branchial Na+/K+-ATPase activity. The latter effect was interpreted as compensation for an elevated chloride and sodium load. The increases in plasma chloride and sodium concentrations were accompanied by a marked suppression of drinking, thereby indicating that acute silver toxicity was likely caused by a combination of elevated electrolyte concentrations and dehydration.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s003600050243
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
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