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Complex environment of nascent polypeptide chains

W J Hansen1, V R Lingappa, W J Welch

  • 1Department of Medicine, University of California, San Francisco 94143.

The Journal of Biological Chemistry
|October 28, 1994
PubMed
Summary

Newly synthesized proteins form large complexes with molecular chaperones like hsp70. These nascent polypeptide complexes are sensitive to ATP, suggesting a cytoplasmic machinery for protein folding.

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Area of Science:

  • Molecular Biology
  • Protein Biochemistry
  • Cellular Biology

Background:

  • Nascent polypeptides associate with proteins during synthesis.
  • Understanding these complexes is crucial for protein folding and cellular function.

Purpose of the Study:

  • Investigate the composition and properties of nascent polypeptide-protein complexes.
  • Elucidate the role of molecular chaperones, specifically hsp70, in these complexes.

Main Methods:

  • Utilized an in vitro translation system with a non-stop mRNA.
  • Employed puromycin treatment to release complexes from polysomes.
  • Performed gel-filtration chromatography to determine complex molecular mass.
  • Assessed ATP sensitivity and protease digestion of complexes.

Main Results:

  • Identified complexes containing nascent polypeptides (<20 kDa), hsp70, and other proteins.
  • Determined the native molecular mass of the complex to be >700 kDa.
  • Demonstrated that ATP disrupts the nascent polypeptide-hsp70 interaction.
  • Observed altered protease sensitivity of nascent chains in the presence of ATP.

Conclusions:

  • Evidence suggests a cytoplasmic machinery involving hsp70 that binds nascent polypeptide chains.
  • This machinery likely plays a role in early protein folding and quality control.
  • ATP-dependent regulation is a key feature of this nascent chain binding complex.

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