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Article ; Online: Knockout of adenylosuccinate synthase purA increases susceptibility to colistin in Escherichia coli.

Kano, Tomonori / Ishikawa, Kazuya / Furuta, Kazuyuki / Kaito, Chikara

2024 Volume 371

Abstract: Colistin is a cationic cyclic antimicrobial peptide used as a last resort against multidrug-resistant gram-negative bacteria. To understand the factors involved in colistin susceptibility, we screened colistin-sensitive mutants from an E. coli gene- ... ...

Abstract	Colistin is a cationic cyclic antimicrobial peptide used as a last resort against multidrug-resistant gram-negative bacteria. To understand the factors involved in colistin susceptibility, we screened colistin-sensitive mutants from an E. coli gene-knockout library (Keio collection). The knockout of purA, whose product catalyzes the synthesis of adenylosuccinate from IMP in the de novo purine synthesis pathway, resulted in increased sensitivity to colistin. Adenylosuccinate is subsequently converted to AMP, which is phosphorylated to produce ADP, a substrate for ATP synthesis. The amount of ATP was lower in the purA-knockout mutant than that in the wild-type strain. ATP synthesis is coupled with proton transfer, and it contributes to the membrane potential. Using the membrane potential probe, 3,3'-diethyloxacarbocyanine iodide [DiOC2(3)], we found that the membrane was hyperpolarized in the purA-knockout mutant compared to that in the wild-type strain. Treatment with the proton uncoupler, carbonyl cyanide m-chlorophenyl hydrazone (CCCP), abolished the hyperpolarization and colistin sensitivity in the mutant. The purA-knockout mutant exhibited increased sensitivity to aminoglycosides, kanamycin, and gentamicin; their uptake requires a membrane potential. Therefore, the knockout of purA, an adenylosuccinate synthase, decreases ATP synthesis concurrently with membrane hyperpolarization, resulting in increased sensitivity to colistin.
MeSH term(s)	Adenylosuccinate Synthase ; Escherichia coli/genetics ; Colistin/pharmacology ; Protons ; Anti-Bacterial Agents/pharmacology ; Carbonyl Cyanide m-Chlorophenyl Hydrazone/pharmacology ; Adenosine Triphosphate ; Microbial Sensitivity Tests
Chemical Substances	Adenylosuccinate Synthase (EC 6.3.4.4) ; Colistin (Z67X93HJG1) ; Protons ; Anti-Bacterial Agents ; Carbonyl Cyanide m-Chlorophenyl Hydrazone (555-60-2) ; Adenosine Triphosphate (8L70Q75FXE)
Language	English
Publishing date	2024-02-21
Publishing country	England
Document type	Journal Article
ZDB-ID	752343-9
ISSN	1574-6968 ; 0378-1097
ISSN (online)	1574-6968
ISSN	0378-1097
DOI	10.1093/femsle/fnae007
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Article ; Online: Overexpression of the flagellar motor protein MotB sensitizes Bacillus subtilis to aminoglycosides in a motility-independent manner.

Uneme, Mio / Ishikawa, Kazuya / Furuta, Kazuyuki / Yamashita, Atsuko / Kaito, Chikara

PloS one

2024 Volume 19, Issue 4, Page(s) e0300634

Abstract: The flagellar motor proteins, MotA and MotB, form a complex that rotates the flagella by utilizing the proton motive force (PMF) at the bacterial cell membrane. Although PMF affects the susceptibility to aminoglycosides, the effect of flagellar motor ... ...

Abstract	The flagellar motor proteins, MotA and MotB, form a complex that rotates the flagella by utilizing the proton motive force (PMF) at the bacterial cell membrane. Although PMF affects the susceptibility to aminoglycosides, the effect of flagellar motor proteins on the susceptibility to aminoglycosides has not been investigated. Here, we found that MotB overexpression increased susceptibility to aminoglycosides, such as kanamycin and gentamicin, in Bacillus subtilis without affecting swimming motility. MotB overexpression did not affect susceptibility to ribosome-targeting antibiotics other than aminoglycosides, cell wall-targeting antibiotics, DNA synthesis-inhibiting antibiotics, or antibiotics inhibiting RNA synthesis. Meanwhile, MotB overexpression increased the susceptibility to aminoglycosides even in the motA-deletion mutant, which lacks swimming motility. Overexpression of the MotB mutant protein carrying an amino acid substitution at the proton-binding site (D24A) resulted in the loss of the enhanced aminoglycoside-sensitive phenotype. These results suggested that MotB overexpression sensitizes B. subtilis to aminoglycosides in a motility-independent manner. Notably, the aminoglycoside-sensitive phenotype induced by MotB requires the proton-binding site but not the MotA/MotB complex formation.
MeSH term(s)	Bacillus subtilis/genetics ; Bacillus subtilis/drug effects ; Bacillus subtilis/metabolism ; Bacterial Proteins/metabolism ; Bacterial Proteins/genetics ; Aminoglycosides/pharmacology ; Anti-Bacterial Agents/pharmacology ; Flagella/metabolism ; Flagella/drug effects ; Molecular Motor Proteins/metabolism ; Molecular Motor Proteins/genetics
Chemical Substances	Bacterial Proteins ; Aminoglycosides ; MotB protein, Bacteria ; Anti-Bacterial Agents ; MotA protein, Bacteria ; Molecular Motor Proteins
Language	English
Publishing date	2024-04-26
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2267670-3
ISSN	1932-6203 ; 1932-6203
ISSN (online)	1932-6203
ISSN	1932-6203
DOI	10.1371/journal.pone.0300634
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Article ; Online: Knockout of ribosomal protein RpmJ leads to zinc resistance in Escherichia coli.

Shirakawa, Riko / Ishikawa, Kazuya / Furuta, Kazuyuki / Kaito, Chikara

PloS one

2023 Volume 18, Issue 3, Page(s) e0277162

Abstract: Zinc is an essential metal for cells, but excess amounts are toxic. Other than by regulating the intracellular zinc concentration by zinc uptake or efflux, the mechanisms underlying bacterial resistance to excess zinc are unknown. In the present study, ... ...

Abstract	Zinc is an essential metal for cells, but excess amounts are toxic. Other than by regulating the intracellular zinc concentration by zinc uptake or efflux, the mechanisms underlying bacterial resistance to excess zinc are unknown. In the present study, we searched for zinc-resistant mutant strains from the Keio collection, a gene knockout library of Escherichia coli, a model gram-negative bacteria. We found that knockout mutant of RpmJ (L36), a 50S ribosomal protein, exhibited zinc resistance. The rpmJ mutant was sensitive to protein synthesis inhibitors and had altered translation fidelity, indicating ribosomal dysfunction. In the rpmJ mutant, the intracellular zinc concentration was decreased under excess zinc conditions. Knockout of ZntA, a zinc efflux pump, abolished the zinc-resistant phenotype of the rpmJ mutant. RNA sequence analysis revealed that the rpmJ mutant exhibited altered gene expression of diverse functional categories, including translation, energy metabolism, and stress response. These findings suggest that knocking out RpmJ alters gene expression patterns and causes zinc resistance by lowering the intracellular zinc concentration. Knockouts of other ribosomal proteins, including RplA, RpmE, RpmI, and RpsT, also led to a zinc-resistant phenotype, suggesting that deletion of ribosomal proteins is closely related to zinc resistance.
MeSH term(s)	Ribosomal Proteins/genetics ; Ribosomal Proteins/metabolism ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Zinc/metabolism ; Ribosomes/genetics ; Ribosomes/metabolism ; Metals/metabolism ; Escherichia coli Proteins/genetics ; Escherichia coli Proteins/metabolism
Chemical Substances	Ribosomal Proteins ; Zinc (J41CSQ7QDS) ; Metals ; Escherichia coli Proteins
Language	English
Publishing date	2023-03-24
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2267670-3
ISSN	1932-6203 ; 1932-6203
ISSN (online)	1932-6203
ISSN	1932-6203
DOI	10.1371/journal.pone.0277162
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Article ; Online: Roles of IgE and Histamine in Mast Cell Maturation.

Tanaka, Satoshi / Furuta, Kazuyuki

Cells

2021 Volume 10, Issue 8

Abstract: Mast cells are activated upon immunoglobulin E (IgE)-mediated antigen stimulation, and release a wide variety of mediators, including histamine to trigger inflammatory responses. The surface expression levels of Fcε receptor I (FcεRI), a high affinity ... ...

Abstract	Mast cells are activated upon immunoglobulin E (IgE)-mediated antigen stimulation, and release a wide variety of mediators, including histamine to trigger inflammatory responses. The surface expression levels of Fcε receptor I (FcεRI), a high affinity receptor of IgE, were found to be positively regulated by IgE. IgE could protect murine cultured mast cells from apoptotic cell death induced by the deprivation of interleukin-3 and a certain kind of IgE could activate immature mast cells in the absence of antigens, leading to the release of pro-inflammatory cytokines and a transient increase in histamine synthesis. Histamine synthesis in mast cells was found to be required for the maturation of murine connective tissue-type mast cells, raising the possibility that IgE indirectly modulates local mast cell maturation. Although it remains controversial to what extent this concept of "monomeric IgE effects" could have relevance in the modulation of human mast cell functions, the therapeutic effects of anti-IgE antibodies might be accounted for in terms of the decreased serum IgE concentrations. Because drastic increases in serum IgE concentrations are often observed in patients with atopic dermatitis and chronic urticaria, a close investigation of the roles of IgE in mast cell maturation should contribute to development of novel therapeutic approaches for these inflammatory diseases.
MeSH term(s)	Histamine/metabolism ; Humans ; Hypersensitivity/metabolism ; Immunoglobulin E/metabolism ; Inflammation/metabolism ; Mast Cells/metabolism ; Nerve Tissue Proteins/metabolism ; Receptors, G-Protein-Coupled/metabolism ; Receptors, Neuropeptide/metabolism
Chemical Substances	MRGPRX2 protein, human ; Nerve Tissue Proteins ; Receptors, G-Protein-Coupled ; Receptors, Neuropeptide ; Immunoglobulin E (37341-29-0) ; Histamine (820484N8I3)
Language	English
Publishing date	2021-08-23
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2661518-6
ISSN	2073-4409 ; 2073-4409
ISSN (online)	2073-4409
ISSN	2073-4409
DOI	10.3390/cells10082170
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Article ; Online: Knockout of mlaA increases Escherichia coli virulence in a silkworm infection model.

Nasu, Haruka / Shirakawa, Riko / Furuta, Kazuyuki / Kaito, Chikara

PloS one

2022 Volume 17, Issue 7, Page(s) e0270166

Abstract: The mlaA gene encodes a lipoprotein to maintain an outer membrane lipid asymmetry in gram-negative bacteria. Although the role of mlaA in bacterial virulence has been studied in several bacterial species, there are no reports of its role in E. coli ... ...

Abstract	The mlaA gene encodes a lipoprotein to maintain an outer membrane lipid asymmetry in gram-negative bacteria. Although the role of mlaA in bacterial virulence has been studied in several bacterial species, there are no reports of its role in E. coli virulence. In this study, we found that knockout of mlaA in E. coli increased its virulence against silkworms. The mlaA-knockout mutant was sensitive to several antibiotics and detergents, but resistant to vancomycin and chlorhexidine. The mlaA-knockout mutant grew faster than the parent strain in the presence of silkworm hemolymph. The mlaA-knockout mutant also produced a larger amount of outer membrane vesicles than the parent strain. These findings suggest that mlaA knockout causes E. coli resistance to specific antimicrobial substances and increases outer membrane vesicle production, thereby enhancing E. coli virulence properties in the silkworm infection model.
MeSH term(s)	Animals ; Bacterial Outer Membrane Proteins/genetics ; Bombyx/genetics ; Escherichia coli/genetics ; Escherichia coli Infections ; Escherichia coli Proteins/genetics ; Virulence/genetics
Chemical Substances	Bacterial Outer Membrane Proteins ; Escherichia coli Proteins
Language	English
Publishing date	2022-07-13
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2267670-3
ISSN	1932-6203 ; 1932-6203
ISSN (online)	1932-6203
ISSN	1932-6203
DOI	10.1371/journal.pone.0270166
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Article ; Online: Staphylococcus aureus MazG hydrolyzes oxidized guanine nucleotides and contributes to oxidative stress resistance

Nigo, Fuki / Nakagawa, Ryosuke / Hirai, Yuuki / Imai, Lina / Suzuki, Yutaka / Furuta, Kazuyuki / Kaito, Chikara

Biochimie. 2023 June, v. 209 p.52-60

2023

Abstract: We previously reported that knockout of the mazG (SA1292) gene decreases Staphylococcus aureus killing activity against silkworms. S. aureus MazG (SaMazG) has a nucleotide pyrophosphatase domain conserved among MazG family proteins, but its biochemical ... ...

Abstract	We previously reported that knockout of the mazG (SA1292) gene decreases Staphylococcus aureus killing activity against silkworms. S. aureus MazG (SaMazG) has a nucleotide pyrophosphatase domain conserved among MazG family proteins, but its biochemical characteristics are unknown. In the present study, we purified recombinant N-terminal His-tagged SaMazG protein and examined its biochemical activity. SaMazG hydrolyzed GTP, UTP, dGTP, and TTP into nucleoside monophosphates. Hydrolytic activity of SaMazG against ATP, CTP, dATP, and dCTP was low or not detected. SaMazG exhibited high hydrolytic activity against 8-oxo-GTP and 8-oxo-dGTP, oxidized guanine nucleotides, with a Vₘₐₓ/Kₘ ratio more than 15-fold that of GTP. Furthermore, the S. aureus mazG knockout mutant was sensitive to hydrogen peroxide compared with the parent strain. These results suggest that SaMazG is a nucleotide pyrophosphatase hydrolyzing oxidized guanine nucleotides that contributes to the oxidative stress resistance of S. aureus.
Keywords	Staphylococcus aureus ; genes ; guanine nucleotides ; hydrogen peroxide ; mutants ; nucleosides ; oxidation ; oxidative stress ; stress tolerance ; Nucleotide pyrophosphatase ; 8-Oxo-GTP ; MazG
Language	English
Dates of publication	2023-06
Size	p. 52-60.
Publishing place	Elsevier B.V.
Document type	Article ; Online
Note	Pre-press version
ZDB-ID	120345-9
ISSN	0300-9084
ISSN	0300-9084
DOI	10.1016/j.biochi.2023.02.001
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Article: [Regulation of cell surface expression of MHC-II in dendritic cells].

Furuta, Kazuyuki

Seikagaku. The Journal of Japanese Biochemical Society

2014 Volume 86, Issue 1, Page(s) 72–76

MeSH term(s)	Animals ; Biological Transport ; Cell Membrane/metabolism ; Dendritic Cells/cytology ; Dendritic Cells/metabolism ; Genes, MHC Class II/physiology ; Humans ; Membrane Proteins/immunology ; Membrane Proteins/metabolism ; T-Lymphocytes/cytology ; T-Lymphocytes/metabolism
Chemical Substances	Membrane Proteins
Language	Japanese
Publishing date	2014-02
Publishing country	Japan
Document type	Journal Article ; Review
ZDB-ID	282319-6
ISSN	0037-1017
ISSN	0037-1017
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Zs.B 592: Show issues

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Article ; Online: ATP and its metabolite adenosine cooperatively upregulate the antigen-presenting molecules on dendritic cells leading to IFN-γ production by T cells.

Furuta, Kazuyuki / Onishi, Hiroka / Ikada, Yuki / Masaki, Kento / Tanaka, Satoshi / Kaito, Chikara

The Journal of biological chemistry

2023 Volume 299, Issue 4, Page(s) 104587

Abstract: Dendritic cells (DCs) present foreign antigens to T cells via the major histocompatibility complex (MHC), thereby inducing acquired immune responses. ATP accumulates at sites of inflammation or in tumor tissues, which triggers local inflammatory ... ...

Abstract	Dendritic cells (DCs) present foreign antigens to T cells via the major histocompatibility complex (MHC), thereby inducing acquired immune responses. ATP accumulates at sites of inflammation or in tumor tissues, which triggers local inflammatory responses. However, it remains to be clarified how ATP modulates the functions of DCs. In this study, we investigated the effects of extracellular ATP on mouse bone marrow-derived dendritic cells (BMDCs) as well as the potential for subsequent T cell activation. We found that high concentrations of ATP (1 mM) upregulated the cell surface expression levels of MHC-I, MHC-II, and co-stimulatory molecules CD80 and CD86 but not those of co-inhibitory molecules PD-L1 and PD-L2 in BMDCs. Increased surface expression of MHC-I, MHC-II, CD80, and CD86 was inhibited by a pan-P2 receptor antagonist. In addition, the upregulation of MHC-I and MHC-II expression was inhibited by an adenosine P1 receptor antagonist and by inhibitors of CD39 and CD73, which metabolize ATP to adenosine. These results suggest that adenosine is required for the ATP-induced upregulation of MHC-I and MHC-II. In the mixed leukocyte reaction assay, ATP-stimulated BMDCs activated CD4 and CD8T cells and induced interferon-γ (IFN-γ) production by these T cells. Collectively, these results suggest that high concentrations of extracellular ATP upregulate the expression of antigen-presenting and co-stimulatory molecules but not that of co-inhibitory molecules in BMDCs. Cooperative stimulation of ATP and its metabolite adenosine was required for the upregulation of MHC-I and MHC-II. These ATP-stimulated BMDCs induced the activation of IFN-γ-producing T cells upon antigen presentation.
MeSH term(s)	Mice ; Animals ; T-Lymphocytes ; Dendritic Cells ; Antigen Presentation ; Lymphocyte Activation ; Adenosine Triphosphate/metabolism
Chemical Substances	Adenosine Triphosphate (8L70Q75FXE)
Language	English
Publishing date	2023-03-06
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1016/j.jbc.2023.104587
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Article ; Online: Short-chain fatty acids stimulate dendrite elongation in dendritic cells by inhibiting histone deacetylase.

Inamoto, Takuho / Furuta, Kazuyuki / Han, Cheng / Uneme, Mio / Kano, Tomonori / Ishikawa, Kazuya / Kaito, Chikara

The FEBS journal

2023 Volume 290, Issue 24, Page(s) 5794–5810

Abstract: Dendritic cells activate immune responses by presenting pathogen-derived molecules. The dendrites of dendritic cells contribute to the incorporation of foreign antigens or presenting antigens to T cells. Short-chain fatty acids (SCFAs), such as acetic, ... ...

Abstract	Dendritic cells activate immune responses by presenting pathogen-derived molecules. The dendrites of dendritic cells contribute to the incorporation of foreign antigens or presenting antigens to T cells. Short-chain fatty acids (SCFAs), such as acetic, propionic, butyric and valeric acids, have many effects on immune responses by activating specific receptors or inhibiting a histone deacetylase (HDAC), although their effect on dendrite formation in dendritic cells is unknown. In the present study, we aimed to investigate the effect of SCFAs on dendrite elongation using a dendritic cell line (DC2.4 cells) and mouse bone marrow-derived dendritic cells. We found that SCFAs induced dendrite elongation. The elongation was reduced by inhibitors of Src family kinase (SFK), phosphatidylinositol-3 kinase (PI3K), Rho family GTPases (Cdc42, Rac1) or actin polymerization, indicating that SCFAs promote dendrite elongation by activating actin polymerization via the SFK/PI3K/Rho family GTPase signaling pathway. We showed that agonists for SCFA receptors GPR43 and GPR109a did not promote dendrite elongation. By contrast, HDAC inhibitors, including trichostatin A, promoted dendrite elongation in DC2.4 cells, and the promoting activity of trichostatin A was decreased by inhibiting the SFK/PI3K/Rho family GTPase signaling pathway or actin polymerization. Furthermore, DC2.4 cells treated with valeric acid showed enhanced uptake of soluble proteins, insoluble beads and Staphylococcus aureus. We also found that treatment with valeric acid enhanced major histocompatibility complex class II-mediated antigen presentation in bone marrow-derived dendritic cells. These results suggest that SCFAs promote dendrite elongation by inhibiting HDAC, stimulating the SFK/PI3K/Rho family pathway and activating actin polymerization, resulting in increased antigen uptake and presentation in dendritic cells.
MeSH term(s)	Mice ; Animals ; Actins/metabolism ; Histone Deacetylases/metabolism ; Fatty Acids, Volatile/pharmacology ; rho GTP-Binding Proteins/metabolism ; Dendrites/metabolism ; Dendritic Cells ; Phosphatidylinositol 3-Kinases/metabolism
Chemical Substances	n-pentanoic acid (GZK92PJM7B) ; trichostatin A (3X2S926L3Z) ; Actins ; Histone Deacetylases (EC 3.5.1.98) ; Fatty Acids, Volatile ; rho GTP-Binding Proteins (EC 3.6.5.2) ; Phosphatidylinositol 3-Kinases (EC 2.7.1.-)
Language	English
Publishing date	2023-09-11
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2173655-8
ISSN	1742-4658 ; 1742-464X
ISSN (online)	1742-4658
ISSN	1742-464X
DOI	10.1111/febs.16945
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Article ; Online: Staphylococcus aureus MazG hydrolyzes oxidized guanine nucleotides and contributes to oxidative stress resistance.

Nigo, Fuki / Nakagawa, Ryosuke / Hirai, Yuuki / Imai, Lina / Suzuki, Yutaka / Furuta, Kazuyuki / Kaito, Chikara

Biochimie

2023 Volume 209, Page(s) 52–60

Abstract	We previously reported that knockout of the mazG (SA1292) gene decreases Staphylococcus aureus killing activity against silkworms. S. aureus MazG (SaMazG) has a nucleotide pyrophosphatase domain conserved among MazG family proteins, but its biochemical characteristics are unknown. In the present study, we purified recombinant N-terminal His-tagged SaMazG protein and examined its biochemical activity. SaMazG hydrolyzed GTP, UTP, dGTP, and TTP into nucleoside monophosphates. Hydrolytic activity of SaMazG against ATP, CTP, dATP, and dCTP was low or not detected. SaMazG exhibited high hydrolytic activity against 8-oxo-GTP and 8-oxo-dGTP, oxidized guanine nucleotides, with a V
MeSH term(s)	Staphylococcus aureus/metabolism ; Guanine Nucleotides/metabolism ; Amino Acid Sequence ; Escherichia coli/genetics ; Oxidative Stress ; Guanosine Triphosphate/metabolism
Chemical Substances	Guanine Nucleotides ; Guanosine Triphosphate (86-01-1)
Language	English
Publishing date	2023-02-04
Publishing country	France
Document type	Journal Article
ZDB-ID	120345-9
ISSN	1638-6183 ; 0300-9084
ISSN (online)	1638-6183
ISSN	0300-9084
DOI	10.1016/j.biochi.2023.02.001
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