Backbone dynamics of the cytotoxic Ribonuclease α-sarcin by 15N NMR relaxation methods View Full Text


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Article Info

DATE

2002-12

AUTHORS

José Manuel Pérez-Cañadillas, Marc Guenneugues, Ramón Campos-Olivas, Jorge Santoro, Alvaro Martínez del Pozo, José G. Gavilanes, Manuel Rico, Marta Bruix

ABSTRACT

The cytotoxic ribonuclease α-sarcin is a 150-residue protein that inactivates ribosomes by selectively cleaving a single phosphodiester bond in a strictly conserved rRNA loop. In order to gain insights on the molecular basis of its highly specific activity, we have previously determined its solution structure and studied its electrostatics properties. Here, we complement those studies by analysing the backbone dynamics of α-sarcin through measurement of longitudinal relaxation rates R1, off resonance rotating frame relaxation rates R1ρ, and the 15N1HNOE of the backbone amide 15N nuclei at two different magnetic field strengths (11.7 and 17.6 T). The two sets of relaxation parameters have been analysed in terms of the reduced spectral density mapping formalism, as well as by the model-free approach. α-Sarcin behaves as an axial symmetric rotor of the prolate type (D∥/D⊥=1.16 ± 0.02) which tumbles with a correlation time τm of 7.54 ± 0.02 ns. The rotational diffusion properties have been also independently evaluated by hydrodynamic calculations and are in good agreement with the experimental results. The analysis of the internal dynamics reveals that α-sarcin is composed of a rigid hydrophobic core and some exposed segments which undergo fast (ps to ns) internal motions. Slower motions in the μs to ms time scale are less abundant and in some cases can be assigned to specific motional processes. All dynamic data are discussed in relation to the role of some particular residues of α-sarcin in the process of recognition of its ribosomal target. More... »

PAGES

301-316

References to SciGraph publications

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  • 1997-04. Rotational diffusion anisotropy of proteins from simultaneous analysis of 15N and 13Cα nuclear spin relaxation in JOURNAL OF BIOMOLECULAR NMR
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  • 1998-07. An empirical relationship between rotational correlation time and solvent accessible surface area in JOURNAL OF BIOMOLECULAR NMR
  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1023/a:1021698308683

    DOI

    http://dx.doi.org/10.1023/a:1021698308683

    DIMENSIONS

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    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/12522295


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    30 schema:description The cytotoxic ribonuclease α-sarcin is a 150-residue protein that inactivates ribosomes by selectively cleaving a single phosphodiester bond in a strictly conserved rRNA loop. In order to gain insights on the molecular basis of its highly specific activity, we have previously determined its solution structure and studied its electrostatics properties. Here, we complement those studies by analysing the backbone dynamics of α-sarcin through measurement of longitudinal relaxation rates R1, off resonance rotating frame relaxation rates R1ρ, and the 15N1HNOE of the backbone amide 15N nuclei at two different magnetic field strengths (11.7 and 17.6 T). The two sets of relaxation parameters have been analysed in terms of the reduced spectral density mapping formalism, as well as by the model-free approach. α-Sarcin behaves as an axial symmetric rotor of the prolate type (D∥/D⊥=1.16 ± 0.02) which tumbles with a correlation time τm of 7.54 ± 0.02 ns. The rotational diffusion properties have been also independently evaluated by hydrodynamic calculations and are in good agreement with the experimental results. The analysis of the internal dynamics reveals that α-sarcin is composed of a rigid hydrophobic core and some exposed segments which undergo fast (ps to ns) internal motions. Slower motions in the μs to ms time scale are less abundant and in some cases can be assigned to specific motional processes. All dynamic data are discussed in relation to the role of some particular residues of α-sarcin in the process of recognition of its ribosomal target.
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    39 R1ρ
    40 Ribonuclease α
    41 Sarcin behaves
    42 activity
    43 agreement
    44 amide 15N nuclei
    45 analysis
    46 approach
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    92 phosphodiester bond
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