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  • 1995-1999  (2)
  • Cytochrome oxidase  (1)
  • Insertional operator mutation  (1)
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  • 1995-1999  (2)
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  • 1
    Electronic Resource
    Electronic Resource
    Intracellular location of cytochrome oxidase active in vivo in the cyanophytes,Synechocystis sp. PCC6714 andAnacystis nidulans Tx20 and R2, grown under various conditions (1995)
    Springer
    Protoplasma 188 (1995), S. 70-77 
    Details
    ISSN: 1615-6102
    Keywords: Cyanophytes ; Cytochrome oxidase ; Electron transport ; DAB oxidation ; Respiration
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Intracellular location of cytochrome oxidase (cytoxidase) active in vivo was studied cytochemically with four strains of cyanophytes, using 3,3′-diaminobenzidine (DAB) oxidation. DAB was oxidized in the dark bySynechocystis sp. PCC6714 and two strains ofAnacystis nidulans (Tx20 and R2) grown under photoautotrophic, heterotrophic and salt-stressed conditions, respectively. Electron microscopic observations showed that DAB-oxidation in the dark occurred in the thylakoids, but was insignificant on or around the cytoplasmic membrane. However, deposition of DAB-oxidation product around the cytoplasmic membrane was observed with cells of the thylakoid-less cyanophyteGlaeobacter violaceus ATCC29082. All DAB oxidations observed with the four strains were inhibited completely by cyanide, the inhibitor of cyt-oxidase, but not by 3-amino-1,2,4-triazole, the inhibitor of peroxidase. The results show that (1) DAB was oxidized by the cyt-oxidase functioning in the respiratory system, and that (2) cyt-oxidase in thylakoids was active in vivo.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01276797
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Analysis of an insertional operator mutation (gntOi) that affects the expression level of theBacillus subtilis gnt operon, and characterization ofgntOi suppressor mutations (1995)
    Springer
    Molecular genetics and genomics 248 (1995), S. 583-591 
    Details
    ISSN: 1617-4623
    Keywords: Bacillus subtilis ; gnt operon ; Transcriptional repressor ; Insertional operator mutation ; GntR family
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract TheBacillus subtilis gnt operon is negatively regulated via interaction of thegnt repressor (GntR) with an operator upstream ofgntR, which is antagonized by gluconate. An 8 bp insertional operator mutation (gntOi) of thegnt operon was constructed which affected the expression level of this operon. Two suppressors of thisgntOi mutation, exhibiting normal expression, were also isolated; one involved a threonine substitution for the Ala-48 residue (gntR48T) within the helix-turn-helix DNA-binding motif of GntR, and the other an adenine substitution for the guanine at nucleotide — 4 within thegntOi operator (gntOiM4A) (+1 is the transcription initiation site). ThegntR48T mutation by itself rendered thegnt operon partially constitutive. When thegntR43L mutation, which renders thegnt operon fully constitutive, was introduced into thegntOi orgntOiM4A mutant, the operator mutations were found not to affect the promoter activity of thegnt operon. These in vivo results indicate that thegntOi mutation affects the operator interaction with GntR, causing a low expression level even in the presence of gluconate. In vitro gel retardation and DNase I footprint analyses demonstrated that even when gluconate was present, GntR still bound to thegntOi operator region.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02423454
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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