DOI: 10.1128/jb.184.19.5323-5329.2002. MazG, a Nucleoside Triphosphate Pyrophosphohydrolase, Interacts with Era, an Essential GTPase in<i>Escherichia coli</i>

MazG, a Nucleoside Triphosphate Pyrophosphohydrolase, Interacts with Era, an Essential GTPase inEscherichia coli

10.1128/jb.184.19.5323-5329.2002

Crossref journal-article

American Society for Microbiology

Journal of Bacteriology (235)

Abstract

ABSTRACTEra is an essential GTPase inEscherichia coli, and Era has been implicated in a number of cellular functions. Homologues of Era have been identified in various bacteria and some eukaryotes. Using theeragene as bait in the yeast two-hybrid system to screenE. coligenomic libraries, we discovered that Era interacts with MazG, a protein of unknown function which is highly conserved among bacteria. The direct interaction between Era and MazG was also confirmed in vitro, being stronger in the presence of GDP than in the presence of GTPγS. MazG was characterized as a nucleoside triphosphate pyrophosphohydrolase which can hydrolyze all eight of the canonical ribo- and deoxynucleoside triphosphates to their respective monophosphates and PPi, with a preference for deoxynucleotides. AmazGdeletion strain ofE. coliwas constructed by replacing themazGgene with a kanamycin resistance gene. UnlikemutT, a gene for another conserved nucleotide triphosphate pyrophosphohydrolase that functions as a mutator gene, themazGdeletion did not result in a mutator phenotype inE. coli.

Bibliography

Zhang, J., & Inouye, M. (2002). MazG, a Nucleoside Triphosphate Pyrophosphohydrolase, Interacts with Era, an Essential GTPase inEscherichia coli. Journal of Bacteriology, 184(19), 5323â5329.

Authors 2

Junjie Zhang (first)
Masayori Inouye (additional)

References 32 Referenced 73

Dates

Type	When
Created	22 years, 6 months ago (Feb. 6, 2003, 9:23 p.m.)
Deposited	1 year, 8 months ago (Jan. 6, 2024, 3:16 p.m.)
Indexed	3 months, 2 weeks ago (May 17, 2025, 9:33 p.m.)
Issued	22 years, 11 months ago (Oct. 1, 2002)
Published	22 years, 11 months ago (Oct. 1, 2002)
Published Print	22 years, 11 months ago (Oct. 1, 2002)

Funders 0

None

BibTeX

@article{Zhang_2002, title={MazG, a Nucleoside Triphosphate Pyrophosphohydrolase, Interacts with Era, an Essential GTPase inEscherichia coli}, volume={184}, ISSN={1098-5530}, url={http://dx.doi.org/10.1128/jb.184.19.5323-5329.2002}, DOI={10.1128/jb.184.19.5323-5329.2002}, number={19}, journal={Journal of Bacteriology}, publisher={American Society for Microbiology}, author={Zhang, Junjie and Inouye, Masayori}, year={2002}, month=oct, pages={5323–5329} }

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      "journal-title": "Proc. Natl. Acad. Sci. USA"
    },
    {
      "key": "e_1_3_2_3_2",
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      "volume": "93",
      "year": "1996",
      "unstructured": "Aizenman, E., H. Engelberg-Kulka, and G. Glaser. 1996. An Escherichia coli chromosomal \u201caddiction module\u201d regulated by guanosine [corrected] 3\u2032,5\u2032-bispyrophosphate: a model for programmed bacterial cell death. Proc. Natl. Acad. Sci. USA93:6059-6063.",
      "journal-title": "Proc. Natl. Acad. Sci. USA"
    },
    {
      "key": "e_1_3_2_4_2",
      "doi-asserted-by": "crossref",
      "first-page": "987",
      "DOI": "10.1046/j.1365-2443.2001.00480.x",
      "volume": "6",
      "year": "2001",
      "unstructured": "Akiyama, T., J. Gohda, S. Shibata, Y. Nomura, S. Azuma, Y. Ohmori, S. Sugano, H. Arai, T. Yamamoto, and J. Inoue. 2001. Mammalian homologue of E. coli Ras-like GTPase (ERA) is a possible apoptosis regulator with RNA binding activity. Genes Cells6:987-1001.",
      "journal-title": "Genes Cells"
    },
    {
      "key": "e_1_3_2_5_2",
      "doi-asserted-by": "crossref",
      "first-page": "769",
      "DOI": "10.1016/S0021-9258(19)67936-6",
      "volume": "235",
      "year": "1960",
      "unstructured": "Ames, B. N., and D. T. Dubin. 1960. The role of polyamines in the neutralization of bacteriophage deoxyribonucleic acids. J. Biol. Chem.235:769-775.",
      "journal-title": "J. Biol. Chem."
    },
    {
      "key": "e_1_3_2_6_2",
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      "DOI": "10.1016/S0021-9258(18)31550-3",
      "volume": "266",
      "year": "1991",
      "unstructured": "Bhatnagar, S. K., L. C. Bullions, and M. J. Bessman. 1991. Characterization of the mutT nucleoside triphosphatase of Escherichia coli. J. Biol. Chem.266:9050-9054.",
      "journal-title": "J. Biol. Chem."
    },
    {
      "key": "e_1_3_2_8_2",
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    },
    {
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      "doi-asserted-by": "crossref",
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      "DOI": "10.1074/jbc.M104455200",
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    },
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      "journal-title": "J. Mol. Biol."
    },
    {
      "key": "e_1_3_2_22_2",
      "doi-asserted-by": "crossref",
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      "DOI": "10.1038/355273a0",
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      "journal-title": "Nature"
    },
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      "doi-asserted-by": "crossref",
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      "DOI": "10.1111/j.1365-2958.1992.tb00845.x",
      "volume": "6",
      "year": "1992",
      "unstructured": "March, P. E. 1992. Membrane-associated GTPases in bacteria. Mol. Microbiol.6:1253-1257.",
      "journal-title": "Mol. Microbiol."
    },
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      "key": "e_1_3_2_24_2",
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      "volume": "2",
      "year": "1988",
      "unstructured": "March, P. E., C. G. Lerner, J. Ahnn, X. Cui, and M. Inouye. 1988. The Escherichia coli Ras-like protein (Era) has GTPase activity and is essential for cell growth. Oncogene2:539-544.",
      "journal-title": "Oncogene"
    },
    {
      "key": "e_1_3_2_25_2",
      "doi-asserted-by": "publisher",
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      "volume": "271",
      "year": "1996",
      "unstructured": "O'Handley, S. F., D. N. Frick, L. C. Bullions, A. S. Mildvan, and M. J. Bessman. 1996. Escherichia coli orf17 codes for a nucleoside triphosphate pyrophosphohydrolase member of the MutT family of proteins. Cloning, purification, and characterization of the enzyme. J. Biol. Chem.271:24649-24654.",
      "journal-title": "J. Biol. Chem."
    },
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      "key": "e_1_3_2_27_2",
      "doi-asserted-by": "crossref",
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      "journal-title": "FEMS Microbiol. Lett."
    },
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      "key": "e_1_3_2_28_2",
      "doi-asserted-by": "publisher",
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      "unstructured": "Powell, B. S., D. L. Court, T. Inada, Y. Nakamura, V. Michotey, X. Cui, A. Reizer, M. H. Saier, Jr., and J. Reizer. 1995. Novel proteins of the phosphotransferase system encoded within the rpoN operon of Escherichia coli. Enzyme IIANtr affects growth on organic nitrogen and the conditional lethality of an erats mutant. J. Biol. Chem.270:4822-4839.",
      "journal-title": "J. Biol. Chem."
    },
    {
      "key": "e_1_3_2_30_2",
      "doi-asserted-by": "crossref",
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      "DOI": "10.1006/bbrc.1999.1471",
      "volume": "264",
      "year": "1999",
      "unstructured": "Sayed, A., S. Matsuyama, and M. Inouye. 1999. Era, an essential Escherichia coli small G-protein, binds to the 30S ribosomal subunit. Biochem. Biophys. Res. Commun.264:51-54.",
      "journal-title": "Biochem. Biophys. Res. Commun."
    },
    {
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    },
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