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1H, 15N and 13C chemical shift assignments of the C-Ala domain of the alanyl-tRNA synthetase of the psychrophilic bacterium Bizionia argentinensis sp. nov.

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Abstract

A gene encoding a protein classified as alanyl-tRNA synthetase (AlaRS) was found in the genome of the psychrophilic bacteria Bizionia argentinensis. The enzyme is constituted by three domains with an evolutionarily conserved modular arrangement: the N-terminal aminoacylation domain, the editing domain and the C-terminal domain (C-Ala). Herein we report the near complete NMR resonance assignment of the 122 amino acid C-Ala domain from B. argentinensis. The chemical shift data, reported for the first time for a C-Ala domain, constitute the basis for NMR structural studies aimed at elucidating the cold-adaptation mechanism of AlaRS.

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Acknowledgments

C.S. acknowledges financial support by Fundación Bunge Born and the 2011 Cooperint Internationalization Program of the University of Verona.

Conflict of interest

The authors declare that they have no conflict of interest.

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Authors and Affiliations

  1. Fundación Instituto Leloir, Patricias Argentinas 435, C1405BWE, Buenos Aires, Argentina

    Clara Smal

  2. Dipartimento di Biotecnologie, Università di Verona, Strada Le Grazie 15, 37134, Verona, Italy

    Clara Smal, Serena Zanzoni, Mariapina D’Onofrio & Michael Assfalg

  3. CNR-ISMAC, Via Bassini 15, 20133, Milan, Italy

    Henriette Molinari

  4. Dipartimento di Scienze e Tecnologie Chimiche, Università di Roma “Tor Vergata”, Via della Ricerca Scientifica SNC, 00133, Rome, Italy

    Daniel O. Cicero

Authors
  1. Clara Smal
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  2. Serena Zanzoni
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  3. Mariapina D’Onofrio
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  4. Henriette Molinari
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  5. Daniel O. Cicero
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  6. Michael Assfalg
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Corresponding authors

Correspondence to Daniel O. Cicero or Michael Assfalg.

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Smal, C., Zanzoni, S., D’Onofrio, M. et al. 1H, 15N and 13C chemical shift assignments of the C-Ala domain of the alanyl-tRNA synthetase of the psychrophilic bacterium Bizionia argentinensis sp. nov.. Biomol NMR Assign 8, 415–418 (2014). https://doi.org/10.1007/s12104-013-9529-8

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  • DOI: https://doi.org/10.1007/s12104-013-9529-8

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