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Yoshikatsu Murooka Masanao Oda Yasuo Kobayashi 《Applied microbiology and biotechnology》1986,24(6):499-503
Summary We have constructed promoter probe vectors with the Escherichia coli galactokinase monitoring system that can be used in Bacillus subtilis. In vivo studies with these vectors demonstrated that the E. coli trp and tac(trp::lac) promoter regions could be utilized in B. subtilis. These promoter regions and the promoter region for the erythromycin resistance gene originating from Staphylococcus aureus were preferentially utilized during the stationary growth phase of B. subtilis, whereas the B. subtilis P21K and P29K promoters were utilized during the exponential growth phase and decreased rapidly during the stationary phase. The apparent strength of these promoters of E. coli in B. subtilis, in terms of galactokinase units, was comparable with those of the B. subtilis promoters. 相似文献
3.
Poly(ADP-ribose) polymerase cDNAs have been isolated from different classes of animals. Cloning of genes from lower eukaryotes has allowed us to investigate directly the biological functions of poly(ADP-ribosyl)ationin vivo. The conservation of specific regions among mammals, chicken,Xenopus laevis, andDrosophila melanogaster reveals the essential structural elements required for recognition of breaks in DNA and for catalytic activity. Cys, His and basic residues in the zinc-finger consensus region are conserved. The carboxyl terminal region corresponding to an NAD-binding domain is strongly conserved. The dinucleotide-binding consensus sequence and 1-A-2, Rossmann fold structure, and -sheet structures are completely conserved from mammals to insect. InDrosophila, a putative leucine-zipper motif has been identified, and other poly(ADP-ribose) polymerases also contain an -helical, amphipathic structure in the auto-modification domain. In this article, we review the recent structural analyses of the functional domains of poly(ADP-ribose) polymerase in phylogenetically divergent species, and discuss the implications of structural conservation for its biological functions.Abbreviations aa
amino acid(s)
-
D. melanogaster
Drosophila melanogaster
- PARP
poly(ADP-ribose) polymerase [EC 2.4.2.30]
- PCR
polymerase chain reaction
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X. laevis
Xenopus laevis 相似文献
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Minoru Yoshida Hiroshi Morimoto Masanao Matsui Ryohei Oda 《Bioscience, biotechnology, and biochemistry》2013,77(9):1314-1319
Biological availability of 33 esters, 17 ethers and 2 acetals of ethanediol, 1,2-propanediol, 1,3-butanediol and 1,4-butanediol was compared by mini-test with chicks. Chicks can utilize esters of ethanediol, 1,2-propanediol and 1,3-butanediol with acetic acid and fatty acids of carbon chain length from 5 to 12 with more improved palatability than that of free acids, while availability of esters of these glycols with propionic and butyric acids was low. Esters of 1,4-butanediol and ether derivatives of these glycols was not available, except ethyl ether of di-ethanediol which was partially available. Acetacetal of ethanediol was partially available but n-butyracetal was not. 相似文献
7.
Temperature dependence of proton nuclear magnetic resonance spectra has been followed for cobrotoxin, a postsynaptic neurotoxin fromNaja naja atra venom. Several aromatic amino-acid residues, including the functionally essential Trp-29 located at the tip of the central loop of the molecule, have been found to undergo a thermal structural transition above the global thermal denaturation temperature. It is suggested that a local structure around these residues behaves somehow independently of the rest of the molecule, and that such structural organization may be favorable for a conformational change of a neurotoxin molecule on binding to acetylcholine receptor. 相似文献
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Poly(ADP-ribose): Historical perspective 总被引:2,自引:0,他引:2
10.
Masayuki Sakakibara Kenji Mori Masanao Matsui 《Bioscience, biotechnology, and biochemistry》2013,77(10):1825-1827
Several microorganisms capable of utilizing 1-aminocyclopropane-1-carboxylate (ACPC) were isolated from soil. A bacterium which belongs to Pseudomonas accumulated cellular α-aminobutyrate with consumption of ACPC and cells incubated with ACPC medium had the activity deaminating the substrate to form α-ketobutyrate. An enzyme, ACPC deaminase, was highly purified and its molecular weight, substrate specificity and absorption spectrum were investigated. These results suggested that this enzyme was a pyridoxal 5′-phosphate enzyme which has the molecular weight of 104000 and high specificity for ACPC, Km= 1.5 mM. A yeast, Hansenula saturnus, is also capable of forming ACPC deaminase, which has a lower molecular weight, 69000, and higher Km value, 2.6 mM. 相似文献