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Related Experiment Videos

Transformation by p60src with altered N-terminal sequences.

H Hanafusa1, E A Garber, T Hanafusa

  • 1Rockefeller University, New York, New York 10021.

Princess Takamatsu Symposia
|January 1, 1986
PubMed
Summary
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Altered src proteins from Rous sarcoma virus, lacking myristylation but retaining transforming activity, show unusual N-terminal structures. These modifications correlate with rapid tumor regression, offering insights into viral oncogenesis.

Area of Science:

  • Virology
  • Molecular Biology
  • Oncology

Background:

  • The Rous sarcoma virus src gene product, p60src, requires tyrosine kinase activity and N-terminal myristylation for plasma membrane association and transformation.
  • Myristylation is crucial for p60src's membrane localization and oncogenic function.

Purpose of the Study:

  • To investigate the unusual N-terminal structures of src proteins from recovered avian sarcoma viruses (rASV157 and rASV1702).
  • To determine the role of these altered N-terminal structures in the transforming activity and tumor regression induced by these viruses.

Main Methods:

  • Analysis of the N-terminal amino acid sequences of src proteins from rASV157 and rASV1702.
  • Correlation of structural alterations with observed biological properties, including transforming activity and tumor induction/regression.

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Main Results:

  • Src proteins from rASV157 and rASV1702 lack myristylation but are active in cell transformation.
  • These src proteins possess unique N-terminal structures with 30-45 amino acids from the env signal peptide fused to internal src sequences.
  • These structural anomalies are linked to the rapid regression of tumors induced by these viruses.

Conclusions:

  • The N-terminal modifications of src proteins in rASV157 and rASV1702 are responsible for their oncogenic properties and the observed rapid tumor regression.
  • Myristylation is not essential for src-mediated transformation in these specific viral variants.
  • These findings provide novel insights into the structure-function relationships of viral oncoproteins.