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  • 1
    Electronic Resource
    Electronic Resource
    Interspecies compatibility of selenoprotein biosynthesis in Enterobacteriaceae (1991)
    Springer
    Archives of microbiology 155 (1991), S. 221-228 
    Details
    ISSN: 1432-072X
    Keywords: Selenopolypeptide ; Selenated tRNAs ; Enterobacteriaceae ; UGA decoding ; Functional compatibility
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Several species of Enterobacteriaceae were investigated for their ability to synthesise selenium-containing macromolecules. Selenated tRNA species as well as selenated polypeptides were formed by all organisms tested. Two selenopolypeptides could be identified in most of the organisms which correspond to the 80 kDa and 110 kDa subunits of the anaerobicaly induced formate dehydrogenase isoenzymes of E coli. In those organisms possessing both isoenzymes, their synthesis was induced in a mutually exclusive manner dependent upon whether nitrate was present during anaerobic growth. The similarity of the 80 kDa selenopolypeptide among the different species was assessed by immunollogical and genetic analyses. Antibodies raised against the 80 kDa selenopolypeptide from E. coli cross-reacted with an 80 kDa polypeptide in those organisms which exhibited fermentative formate dehydrogenase activity. These organisms also contained genes which hydridised with the fdhF gene from E. coli. In an attempt to identify the signals responsible for incorporation of selenium into the selenopolypeptides in these organisms we cloned a portion of the fdhF gene homologue from Enterobacter aerogenes. The nucleotide sequence of the cloned 723 bp fragment was determined and it was shown to contain an in-frame TGA (stop) codon at the position corresponding to that present in the E. coli gene. This fragment was able to direct incorporation of selenocysteine when expressed in the heterologous host, E. coli. Moreover, the E. coli fdhF gene was expressed in Salmonella typhimurium, Serratia marcescens and Proteus mirabilis, indicating a high degree of convervation of the selenating system throughout the enterobacteria.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00252204
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    The anaerobic degradation of l-serine and l-threonine in enterobacteria: networks of pathways and regulatory signals (1998)
    Springer
    Archives of microbiology 171 (1998), S. 1-5 
    Details
    ISSN: 1432-072X
    Keywords: Key wordsl-Serine ; l-threonine ; Anaerobiosis ; Pyridoxal 5′-phosphate enzymes ; Iron-sulfur enzymes ; Glycyl radical enzymes ; Metabolism
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The mechanisms controlling the biosynthesis and degradation of l-serine and l-threonine are remarkably complex. Their metabolism forms a network of pathways linking several amino acids, central primary metabolites such as pyruvate, oxaloacetate and 3-phosphoglycerate, and C1 metabolism. Studies on the degradation of these amino acids in Escherichia coli have revealed the involvement of fascinating enzymes that utilise quite diverse catalytic mechanisms. Moreover, it is emerging that both environmental and metabolic signals have a major impact in controlling enzyme synthesis. This is exemplified by the anaerobically regulated tdc operon, which encodes a metabolic pathway for the degradation of serine and threonine. Studies on this pathway are beginning to provide insights into how an organism adapts its genetic makeup to meet the physiological demands of the cell.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002030050670
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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