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Protein dynamics in living cells.

Julie E Bryant1, Juliette T J Lecomte, Andrew L Lee

  • 1Departments of Chemistry, University of North Carolina, Chapel Hill, North Carolina 27599, USA.

Biochemistry
|June 29, 2005
PubMed
Summary

Protein dynamics in living bacteria are similar to dilute solutions. Intracellular viscosity, not altered dynamics, explains most differences observed using in-cell NMR (nuclear magnetic resonance).

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Biophysics

Background:

  • Protein function is linked to structure and dynamics.
  • Protein dynamics are typically studied in vitro under dilute conditions ( < 10 g/L).
  • Intracellular environments are crowded ( > 400 g/L), potentially affecting protein dynamics.

Purpose of the Study:

  • Investigate fast protein dynamics within living Escherichia coli.
  • Assess the biological relevance of in vitro NMR-derived protein dynamics data.
  • Determine if the crowded intracellular environment alters protein dynamics.

Main Methods:

  • Utilized in-cell Nuclear Magnetic Resonance (NMR) spectroscopy.
  • Quantified backbone dynamics of apocytochrome b5 using {1H}-15N nuclear Overhauser effect (nOe) measurements.

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  • Characterized motions on the pico- to nanosecond timescale.

    • Main Results:

    • The overall trend of protein backbone dynamics remained consistent inside living E. coli compared to in vitro studies.
    • Observed differences in {1H}-15N nOe values were primarily attributed to increased intracellular viscosity.
    • No significant alteration in protein dynamics due to the crowded cellular environment was detected.

    Conclusions:

    • Dilute solution steady-state {1H}-15N nOe measurements provide biologically relevant information.
    • Pico- to nanosecond backbone motion in proteins is largely unaffected by the crowded intracellular environment.
    • In-cell NMR confirms the validity of in vitro dynamics studies for understanding protein function in vivo.