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Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy
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Comparison of folding rates of homologous prokaryotic and eukaryotic proteins.

M Widmann1, P Christen

  • 1Biochemisches Institut der Universität Zürich, CH-8057 Zürich, Switzerland.

The Journal of Biological Chemistry
|April 27, 2000
PubMed
Summary

Prokaryotic proteins fold faster than eukaryotic ones, matching their rapid biosynthesis rates. This evolutionary adaptation optimizes protein folding efficiency in prokaryotes.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Evolutionary Biology

Background:

  • Polypeptide chain elongation occurs significantly faster in prokaryotic cells compared to eukaryotic cells.
  • The rate of protein biosynthesis is a critical factor influencing cellular processes and protein function.

Purpose of the Study:

  • To investigate the correlation between the rates of in vitro protein refolding and the differential rates of biosynthesis in prokaryotic and eukaryotic proteins.
  • To determine if evolutionary pressures have adapted protein folding rates to match polypeptide chain elongation rates.

Main Methods:

  • Comparative analysis of in vitro refolding rates for orthologous prokaryotic and eukaryotic proteins, including aspartate aminotransferases, malate dehydrogenase, and lactate dehydrogenase.
  • Denaturation of proteins using 6 M guanidine hydrochloride followed by monitoring refolding at 25 degrees C.
  • Sequence identity and three-dimensional structural comparisons of orthologous proteins.

Main Results:

  • Prokaryotic aspartate aminotransferase refolded approximately 6 times faster than its eukaryotic counterparts (chicken mitochondrial and cytosolic isoenzymes) at 25 degrees C after denaturation.
  • Orthologous prokaryotic malate dehydrogenase and lactate dehydrogenase also exhibited faster renaturation rates compared to their eukaryotic counterparts.
  • Despite high sequence identity (41-48%) and nearly identical structures, significant differences in refolding kinetics were observed.

Conclusions:

  • The rate of in vitro protein refolding directly correlates with the organism's rate of polypeptide chain elongation.
  • Evolutionary adaptation has likely optimized protein folding rates to align with the faster biosynthesis rates in prokaryotes.
  • These findings provide insights into the molecular mechanisms underlying differential protein folding efficiencies across biological domains.