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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Gitel'zon I.I., Fish A.M., Chumakova R.I., Kuznetsov A.M.
Заглавие : Maximum rate of reproduction of bacteria and the possibility of its determination
Место публикации : Doklady Biological Sciences. - 1973. - Vol. 211, Is. 1-6. - С. 321-323. - ISSN 00124966 (ISSN)
Ключевые слова (''Своб.индексиров.''): bacterial growth--berol 185--in vitro study--microorganism--theoretical study--turbidimetry--vibrionaceae
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Illarrionov B.A., Blinov V.M., Douchenko A.P., Protopopova M.V., Karginov V.A., Mertvetsov N.P., Gitelson J.I.
Заглавие : Isolation of bioluminescent functions from Photobacterium leiognathi: analysis of luxA, luxB, luxG and neighboring genes
Место публикации : Gene. - 1990. - Vol. 86, Is. 1. - С. 89-94. - ISSN 03781119 (ISSN)
Ключевые слова (''Своб.индексиров.''): bioluminescence--expression in e. coli--luciferase--molecular evolution--nucleotide sequence--protein alignment--recombinant dna--luciferase--amino acid sequence--article--bioluminescence--fungus--gene structure--genetic engineering--heredity--nonhuman--nucleotide sequence--priority journal--vibrionaceae--acyltransferases--amino acid sequence--bacterial proteins--base sequence--cloning, molecular--dna, bacterial--genes, structural, bacterial--luciferase--luminescence--molecular sequence data--operon--photobacterium--restriction mapping--escherichia coli--fungi--photobacterium leiognathi--vibrio harveyi--vibrionaceae
Аннотация: Genes encoding luminescence of Photobacterium leiognathi have been cloned in Escherichia coli. The luminescent clones were readily apparent. Among them, a clone containing a recombinant plasmid with a 13.5-kb insertion was identified. This DNA fragment contained all of the luminescence-encoding genes. The luciferase-encoding genes (lux) in this DNA fragment were localized. We have sequenced a part of the cloned lux region and identified the luxA, luxB and luxG genes encoding the ? and ? subunits of luciferase and a ? protein with an Mr of 26 180, respectively. The analysis of deduced amino acid sequences and comparison with known luciferase sequences from Vibrio harveyi, indicate the common origin of these proteins. В© 1990.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Gitelson I.I., Kuznetsov A.M., Rodicheva E.K.
Заглавие : Device for the investigation of maximum growth rate of bacteria
Место публикации : Biotechnology Bioengineering Symposium. - 1974. - Vol. 4, Is. II. - С. 857. - ISSN 05726565 (ISSN)
Ключевые слова (''Своб.индексиров.''): bacterial growth--bacterium--berol 185--control system--growth--microorganism--theoretical study--vibrionaceae
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Petushkov V.N., Gibson B.G., Lee J.
Заглавие : Properties of recombinant fluorescent proteins from Photobacterium leiognathi and their interaction with luciferase intermediates
Место публикации : Biochemistry. - 1995. - Vol. 34, Is. 10. - С. 3300-3309. - ISSN 00062960 (ISSN)
Ключевые слова (''Своб.индексиров.''): luciferase--recombinant protein--article--ligand binding--nonhuman--priority journal--protein isolation--protein protein interaction--protein stability--vibrionaceae--bacterial proteins--binding sites--carrier proteins--circular dichroism--flavin mononucleotide--fluorescence polarization--genes, bacterial--kinetics--ligands--luciferase--luminescence--molecular sequence data--photobacterium--recombinant proteins--spectrophotometry--support, u.s. gov't, p.h.s.--photobacterium leiognathi--vibrionaceae
Аннотация: Ligand binding and luciferase interaction properties of the recombinant protein corresponding to the lumazine protein gene (EMBL X56534) of Photobacterium leiognathi have been determined by fluorescence dynamics, circular dichroism, gel filtration, and SDS-PAGE. Scatchard analysis of a fluorescence titration shows that the apoprotein possess one binding site, and at 30В°C the KdS (?M) are as follows: 6,7-dimethyl-8-ribityllumazine, 0.26; riboflavin, 0.53; and much more weakly bound FMN, 30. All holoproteins are highly fluorescent and have absorption spectra distinct from each other and from the free ligands. The longest wavelength absorption maxima are, respectively (nm, 2В°C), 420,463, and 458. Ligand binding produces no change in the far-UV circular dichroism; all have mean residual ellipticity at 210 nm of -6500 deg cm2 dmol-1, the same as the native protein. However, in the bioluminescence reaction only the lumazine holoprotein shows a bioluminescence effect. Fluorescence emission anisotropy decay was used to establish that none of these holoproteins complexed with native luciferase and that the lumazine protein alone formed a 1:1 complex with the luciferase hydroxyflavin fluorescent transient and the luciferase peroxyflavin intermediates, revealed by a dominant channel of anisotropy loss, with rotational correlation time of 2.5 ns, and attributed to excitation transfer from the luciferase flavin donor to the acceptor, the lumazine ligand. The complex stability was sufficient to allow its isolation by FPLC gel filtration and verification by SDS-PAGE. These methods also confirmed the absence of interaction of the holoflavoproteins.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Petushkov V.N., Gibson B.G., Lee J.
Заглавие : The yellow bioluminescence bacterium, Vibrio fischeri Y1, contains a bioluminescence active riboflavin protein in addition to the yellow fluorescence FMN protein
Место публикации : Biochemical and Biophysical Research Communications. - 1995. - Vol. 211, Is. 3. - С. 774-779. - ISSN 0006291X (ISSN) , DOI 10.1006/bbrc.1995.1880
Ключевые слова (''Своб.индексиров.''): riboflavin--article--bioluminescence--fluorescence--nonhuman--priority journal--protein analysis--protein synthesis--vibrio--vibrionaceae--bacterial proteins--chromatography, gel--chromatography, thin layer--flavin mononucleotide--flavoproteins--luminescence--riboflavin--spectrometry, fluorescence--support, u.s. gov't, p.h.s.--vibrio--bacteria (microorganisms)--photobacterium--vibrio--vibrio fischeri
Аннотация: The yellow bioluminescence Y1 strain of Vibrio fischeri can produce a 22 kDa protein with either FMN or riboflavin as a bound fluorophore. Both forms are active for shifting the bioluminescence spectral maximum. The fluorescence spectral distribution of the two proteins differs slightly and the in vivo emission appears to be an equal mixture of the two. The bioluminescence activity of the riboflavin Y1 protein contrasts with the inactivity of the related Photobacterium type.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Petushkov V.N., Ketelaars M., Gibson B.G., Lee J.
Заглавие : Interaction of Photobacterium leiognathi and Vibrio fischeri Y1 luciferases with fluorescent (antenna) proteins: Bioluminescence effects of the aliphatic additive
Место публикации : Biochemistry. - 1996. - Vol. 35, Is. 37. - С. 12086-12093. - ISSN 00062960 (ISSN) , DOI 10.1021/bi9608931
Ключевые слова (''Своб.индексиров.''): luciferase--anisotropy--antenna--article--bioluminescence--complex formation--energy transfer--enzyme active site--enzyme kinetics--nonhuman--priority journal--protein protein interaction--spectroscopy--vibrionaceae--bacterial proteins--carrier proteins--cloning, molecular--dithionite--flavin mononucleotide--kinetics--luciferases--luminescent measurements--luminescent proteins--models, structural--photobacterium--protein binding--protein conformation--recombinant proteins--spectrophotometry--vibrio--bacteria (microorganisms)--photobacterium--photobacterium leiognathi--vibrio fischeri--vibrionaceae
Аннотация: The kinetics of the bacterial bioluminescence reaction is altered in the presence of the fluorescent (antenna) proteins, lumazine protein (LumP) from Photobacterium or the yellow fluorescence proteins (YFP) having FMN or Rf bound, from Vibrio fischeri strain Y1. Depending on reaction conditions, the bioluminescence intensity and its decay rate may be either enhanced or strongly quenched in the presence of the fluorescent proteins. These effects can be simply explained on the basis of the same protein-protein complex model that accounts for the bioluminescence spectral shifts induced by these fluorescent proteins. In such a complex, where the fluorophore evidently is in proximity to the luciferase active site, it is expected that the on off rate of certain aliphatic components of the reaction should be altered with a consequent shift in the equilibria among the luciferase intermediates, as recently elaborated in a kinetic scheme. These aliphatic components are the bioluminescence reaction substrate, tetradecanal or other long-chain aldehyde, its carboxylic acid product, or dodecanol used as a stabilizer of the luciferase peroxyflavin. No evidence can be found for the protein- protein interaction in the absence of the aliphatic component.
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