DOI: 10.1073/pnas.95.22.12832. <i>Thermus thermophilus</i> : A link in evolution of the tRNA-dependent amino acid amidation pathways

Thermus thermophilus : A link in evolution of the tRNA-dependent amino acid amidation pathways

10.1073/pnas.95.22.12832

Crossref journal-article

Proceedings of the National Academy of Sciences

Proceedings of the National Academy of Sciences (341)

Abstract

Thermus thermophilus possesses an aspartyl-tRNA synthetase (AspRS2) able to aspartylate efficiently tRNA Asp and tRNA Asn . Aspartate mischarged on tRNA Asn then is converted into asparagine by an ω amidase that differs structurally from all known asparagine synthetases. However, aspartate is not misincorporated into proteins because the binding capacity of aminoacylated tRNA Asn to elongation factor Tu is only conferred by conversion of aspartate into asparagine. T. thermophilus additionally contains a second aspartyl-tRNA synthetase (AspRS1) able to aspartylate tRNA Asp and an asparaginyl-tRNA synthetase able to charge tRNA Asn with free asparagine, although the organism does not contain a tRNA-independent asparagine synthetase. In contrast to the duplicated pathway of tRNA asparaginylation, tRNA glutaminylation occurs in the thermophile via the usual pathway by using glutaminyl-tRNA synthetase and free glutamine synthesized by glutamine synthetase that is unique. T. thermophilus is able to ensure tRNA aminoacylation by alternative routes involving either the direct pathway or by conversion of amino acid mischarged on tRNA. These findings shed light on the interrelation between the tRNA-dependent and tRNA-independent pathways of amino acid amidation and on the processes involved in fidelity of the aminoacylation systems.

Bibliography

Becker, H. D., & Kern, D. (1998). Thermus thermophilus â¯: A link in evolution of the tRNA-dependent amino acid amidation pathways. Proceedings of the National Academy of Sciences, 95(22), 12832â12837.

Authors 2

Hubert Dominique Becker (first)
Daniel Kern (additional)

References 41 Referenced 122

10.1128/jb.146.1.345-351.1981
10.1128/jb.172.6.3237-3243.1990
10.1093/nar/18.2.305
10.1128/jb.172.8.4593-4602.1990
10.1128/jb.174.4.1299-1306.1992
10.1128/AAC.37.1.32
10.1002/j.1460-2075.1992.tb05384.x
10.1128/jb.179.8.2587-2594.1997
10.3109/10425179109020780
10.1128/jb.173.24.7903-7910.1991
10.1016/S0006-291X(81)80257-4
10.1073/pnas.90.1.302
10.1128/jb.165.1.88-93.1986
10.1038/331187a0
10.1074/jbc.271.25.14856
10.1111/j.1432-1033.1969.tb00788.x
10.1016/S0021-9258(19)39038-6
10.1038/382589b0
10.1126/science.273.5278.1058
10.1038/41483
10.1021/bi970392v
G Keith Journal of Chromatography Library, eds C W Gehrke, K C Kuo (Elsevier, New York), pp. A103–A141 (1990). / Journal of Chromatography Library by Keith G (1990)
10.1006/abio.1995.1359
10.1093/nar/9.18.4669
10.1016/S0021-9258(18)67425-3
10.1128/mcb.7.7.2435-2443.1987
10.1016/S0021-9258(19)38244-4
10.1073/pnas.94.22.11819
10.1111/j.1432-1033.1996.0501u.x
10.1111/j.1432-1033.1980.tb04714.x
10.1073/pnas.95.22.12838
10.1111/j.1432-1033.1976.tb10965.x
10.1111/j.1432-1033.1994.tb19956.x
C Baron, A Böck tRNA: Structure, Biosynthesis and Function, eds D Söll, U L RajBandhary (Am. Soc. Microbiol., Washington, DC), pp. 529–544 (1995). / tRNA: Structure, Biosynthesis and Function by Baron C (1995)
10.1126/science.270.5241.1464
10.1021/bi00214a021
10.1073/pnas.72.5.1909
10.1073/pnas.91.18.8670
10.1007/BF00166615
10.1146/annurev.bi.47.070178.005403
10.1099/00207713-36-3-444

Dates

Type	When
Created	23 years, 1 month ago (July 26, 2002, 10:40 a.m.)
Deposited	3 years, 4 months ago (April 13, 2022, 4:05 p.m.)
Indexed	1 year ago (Aug. 3, 2024, 9:22 a.m.)
Issued	26 years, 10 months ago (Oct. 27, 1998)
Published	26 years, 10 months ago (Oct. 27, 1998)
Published Online	26 years, 10 months ago (Oct. 27, 1998)
Published Print	26 years, 10 months ago (Oct. 27, 1998)

Funders 0

None

BibTeX

@article{Becker_1998, title={Thermus thermophilus  : A link in evolution of the tRNA-dependent amino acid amidation pathways}, volume={95}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.95.22.12832}, DOI={10.1073/pnas.95.22.12832}, number={22}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Becker, Hubert Dominique and Kern, Daniel}, year={1998}, month=oct, pages={12832–12837} }

JSON

{
  "indexed": {
    "date-parts": [
      [
        2024,
        8,
        3
      ]
    ],
    "date-time": "2024-08-03T13:22:25Z",
    "timestamp": 1722691345154
  },
  "reference-count": 41,
  "publisher": "Proceedings of the National Academy of Sciences",
  "issue": "22",
  "content-domain": {
    "domain": [
      "www.pnas.org"
    ],
    "crossmark-restriction": true
  },
  "published-print": {
    "date-parts": [
      [
        1998,
        10,
        27
      ]
    ]
  },
  "abstract": "<jats:p>\n            <jats:italic>Thermus thermophilus</jats:italic>\n            possesses an aspartyl-tRNA synthetase (AspRS2) able to aspartylate efficiently tRNA\n            <jats:sup>Asp</jats:sup>\n            and tRNA\n            <jats:sup>Asn</jats:sup>\n            . Aspartate mischarged on tRNA\n            <jats:sup>Asn</jats:sup>\n            then is converted into asparagine by an \u03c9 amidase that differs structurally from all known asparagine synthetases. However, aspartate is not misincorporated into proteins because the binding capacity of aminoacylated tRNA\n            <jats:sup>Asn</jats:sup>\n            to elongation factor Tu is only conferred by conversion of aspartate into asparagine.\n            <jats:italic>T. thermophilus</jats:italic>\n            additionally contains a second aspartyl-tRNA synthetase (AspRS1) able to aspartylate tRNA\n            <jats:sup>Asp</jats:sup>\n            and an asparaginyl-tRNA synthetase able to charge tRNA\n            <jats:sup>Asn</jats:sup>\n            with free asparagine, although the organism does not contain a tRNA-independent asparagine synthetase. In contrast to the duplicated pathway of tRNA asparaginylation, tRNA glutaminylation occurs in the thermophile via the usual pathway by using glutaminyl-tRNA synthetase and free glutamine synthesized by glutamine synthetase that is unique.\n            <jats:italic>T. thermophilus</jats:italic>\n            is able to ensure tRNA aminoacylation by alternative routes involving either the direct pathway or by conversion of amino acid mischarged on tRNA. These findings shed light on the interrelation between the tRNA-dependent and tRNA-independent pathways of amino acid amidation and on the processes involved in fidelity of the aminoacylation systems.\n          </jats:p>",
  "DOI": "10.1073/pnas.95.22.12832",
  "type": "journal-article",
  "created": {
    "date-parts": [
      [
        2002,
        7,
        26
      ]
    ],
    "date-time": "2002-07-26T14:40:52Z",
    "timestamp": 1027694452000
  },
  "page": "12832-12837",
  "update-policy": "http://dx.doi.org/10.1073/pnas.cm10313",
  "source": "Crossref",
  "is-referenced-by-count": 122,
  "title": "<i>Thermus thermophilus</i>\n            : A link in evolution of the tRNA-dependent amino acid amidation pathways",
  "prefix": "10.1073",
  "volume": "95",
  "author": [
    {
      "given": "Hubert Dominique",
      "family": "Becker",
      "sequence": "first",
      "affiliation": [
        {
          "name": "Unit\u00e9 Propre de Recherche 9002, \u201cStructure des Macromol\u00e9cules Biologiques et M\u00e9canismes de Reconnaissance,\u201d Institut de Biologie Mol\u00e9culaire et Cellulaire du Centre National de la Recherche Scientifique, 15 Rue Ren\u00e9 Descartes, 67084 Strasbourg C\u00e9dex, France"
        }
      ]
    },
    {
      "given": "Daniel",
      "family": "Kern",
      "sequence": "additional",
      "affiliation": [
        {
          "name": "Unit\u00e9 Propre de Recherche 9002, \u201cStructure des Macromol\u00e9cules Biologiques et M\u00e9canismes de Reconnaissance,\u201d Institut de Biologie Mol\u00e9culaire et Cellulaire du Centre National de la Recherche Scientifique, 15 Rue Ren\u00e9 Descartes, 67084 Strasbourg C\u00e9dex, France"
        }
      ]
    }
  ],
  "member": "341",
  "published-online": {
    "date-parts": [
      [
        1998,
        10,
        27
      ]
    ]
  },
  "reference": [
    {
      "key": "e_1_3_3_1_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1128/jb.146.1.345-351.1981"
    },
    {
      "key": "e_1_3_3_2_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1128/jb.172.6.3237-3243.1990"
    },
    {
      "key": "e_1_3_3_3_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1093/nar/18.2.305"
    },
    {
      "key": "e_1_3_3_4_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1128/jb.172.8.4593-4602.1990"
    },
    {
      "key": "e_1_3_3_5_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1128/jb.174.4.1299-1306.1992"
    },
    {
      "key": "e_1_3_3_6_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1128/AAC.37.1.32"
    },
    {
      "key": "e_1_3_3_7_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1002/j.1460-2075.1992.tb05384.x"
    },
    {
      "key": "e_1_3_3_8_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1128/jb.179.8.2587-2594.1997"
    },
    {
      "key": "e_1_3_3_9_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.3109/10425179109020780"
    },
    {
      "key": "e_1_3_3_10_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1128/jb.173.24.7903-7910.1991"
    },
    {
      "key": "e_1_3_3_11_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/S0006-291X(81)80257-4"
    },
    {
      "key": "e_1_3_3_12_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1073/pnas.90.1.302"
    },
    {
      "key": "e_1_3_3_13_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1128/jb.165.1.88-93.1986"
    },
    {
      "key": "e_1_3_3_14_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1038/331187a0"
    },
    {
      "key": "e_1_3_3_15_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1074/jbc.271.25.14856"
    },
    {
      "key": "e_1_3_3_16_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1111/j.1432-1033.1969.tb00788.x"
    },
    {
      "key": "e_1_3_3_17_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/S0021-9258(19)39038-6"
    },
    {
      "key": "e_1_3_3_18_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1038/382589b0"
    },
    {
      "key": "e_1_3_3_19_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1126/science.273.5278.1058"
    },
    {
      "key": "e_1_3_3_20_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1038/41483"
    },
    {
      "key": "e_1_3_3_21_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1021/bi970392v"
    },
    {
      "key": "e_1_3_3_22_2",
      "first-page": "A103",
      "volume-title": "Journal of Chromatography Library",
      "author": "Keith G",
      "year": "1990",
      "unstructured": "G Keith Journal of Chromatography Library, eds C W Gehrke, K C Kuo (Elsevier, New York), pp. A103\u2013A141 (1990)."
    },
    {
      "key": "e_1_3_3_23_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1006/abio.1995.1359"
    },
    {
      "key": "e_1_3_3_24_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1093/nar/9.18.4669"
    },
    {
      "key": "e_1_3_3_25_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/S0021-9258(18)67425-3"
    },
    {
      "key": "e_1_3_3_26_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1128/mcb.7.7.2435-2443.1987"
    },
    {
      "key": "e_1_3_3_27_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/S0021-9258(19)38244-4"
    },
    {
      "key": "e_1_3_3_28_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1073/pnas.94.22.11819"
    },
    {
      "key": "e_1_3_3_29_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1111/j.1432-1033.1996.0501u.x"
    },
    {
      "key": "e_1_3_3_30_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1111/j.1432-1033.1980.tb04714.x"
    },
    {
      "key": "e_1_3_3_31_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1073/pnas.95.22.12838"
    },
    {
      "key": "e_1_3_3_32_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1111/j.1432-1033.1976.tb10965.x"
    },
    {
      "key": "e_1_3_3_33_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1111/j.1432-1033.1994.tb19956.x"
    },
    {
      "key": "e_1_3_3_34_2",
      "first-page": "529",
      "volume-title": "tRNA: Structure, Biosynthesis and Function",
      "author": "Baron C",
      "year": "1995",
      "unstructured": "C Baron, A B\u00f6ck tRNA: Structure, Biosynthesis and Function, eds D S\u00f6ll, U L RajBandhary (Am. Soc. Microbiol., Washington, DC), pp. 529\u2013544 (1995)."
    },
    {
      "key": "e_1_3_3_35_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1126/science.270.5241.1464"
    },
    {
      "key": "e_1_3_3_36_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1021/bi00214a021"
    },
    {
      "key": "e_1_3_3_37_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1073/pnas.72.5.1909"
    },
    {
      "key": "e_1_3_3_38_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1073/pnas.91.18.8670"
    },
    {
      "key": "e_1_3_3_39_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1007/BF00166615"
    },
    {
      "key": "e_1_3_3_40_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1146/annurev.bi.47.070178.005403"
    },
    {
      "key": "e_1_3_3_41_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1099/00207713-36-3-444"
    }
  ],
  "container-title": "Proceedings of the National Academy of Sciences",
  "original-title": [],
  "language": "en",
  "link": [
    {
      "URL": "https://pnas.org/doi/pdf/10.1073/pnas.95.22.12832",
      "content-type": "unspecified",
      "content-version": "vor",
      "intended-application": "similarity-checking"
    }
  ],
  "deposited": {
    "date-parts": [
      [
        2022,
        4,
        13
      ]
    ],
    "date-time": "2022-04-13T20:05:42Z",
    "timestamp": 1649880342000
  },
  "score": 1,
  "resource": {
    "primary": {
      "URL": "https://pnas.org/doi/full/10.1073/pnas.95.22.12832"
    }
  },
  "subtitle": [],
  "short-title": [],
  "issued": {
    "date-parts": [
      [
        1998,
        10,
        27
      ]
    ]
  },
  "references-count": 41,
  "journal-issue": {
    "issue": "22",
    "published-print": {
      "date-parts": [
        [
          1998,
          10,
          27
        ]
      ]
    }
  },
  "alternative-id": [
    "10.1073/pnas.95.22.12832"
  ],
  "URL": "http://dx.doi.org/10.1073/pnas.95.22.12832",
  "relation": {},
  "ISSN": [
    "0027-8424",
    "1091-6490"
  ],
  "subject": [],
  "container-title-short": "Proc. Natl. Acad. Sci. U.S.A.",
  "published": {
    "date-parts": [
      [
        1998,
        10,
        27
      ]
    ]
  },
  "assertion": [
    {
      "value": "1998-06-01",
      "order": 0,
      "name": "received",
      "label": "Received",
      "group": {
        "name": "publication_history",
        "label": "Publication History"
      }
    },
    {
      "value": "1998-08-12",
      "order": 1,
      "name": "accepted",
      "label": "Accepted",
      "group": {
        "name": "publication_history",
        "label": "Publication History"
      }
    },
    {
      "value": "1998-10-27",
      "order": 2,
      "name": "published",
      "label": "Published",
      "group": {
        "name": "publication_history",
        "label": "Publication History"
      }
    }
  ]
}