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C-terminal end of v-src protein interacts with peptide coded by gadd7/adapt15-like RNA in two-hybrid system

O Mizenina1, Y Yanushevich, E Musatkina

  • 1Institute of Carcinogenesis, Cancer Research Center, Moscow, Russia.

FEBS Letters
|February 25, 1998
PubMed

Insights

Researchers identified a protein, vseap1, that interacts with the Rous sarcoma virus (RSV) v-src protein's C-terminal region, impacting cell metastasis. This discovery sheds light on viral oncogenesis and potential therapeutic targets.

Area of Science:

  • Molecular Biology
  • Virology
  • Oncology

Background:

  • Metastatic properties of hamster fibroblasts transformed by Rous sarcoma virus (RSV) are linked to mutations in the v-src carboxy-terminal region.
  • Understanding protein-protein interactions in this region is crucial for elucidating viral oncogenesis.

Purpose of the Study:

  • To identify proteins interacting with the v-src carboxy-terminal region.
  • To investigate the role of these interactions in viral transformation and metastasis.

Main Methods:

  • Yeast two-hybrid system was employed to screen for interacting proteins.
  • In vitro GST-fusion system was used to confirm protein binding.
  • RNA analysis was performed to study gene expression patterns.

Main Results:

  • A cDNA clone, vseap1, was isolated, encoding a protein that specifically binds to the v-src C-terminal region in both yeast cells (in vivo) and in vitro.
  • Vseap1 exhibits 68% homology to RNA-gadd7/adapt15, a gene induced by stressful agents.
  • Two vseap1-specific messenger RNAs were identified: a 0.9-kbp RNA present in all transformed cells and a 3.1-kbp transcript absent in cells with suppressed v-src activity and H2O2 resistance.

Conclusions:

  • The v-src C-terminal region mediates protein-protein interactions, with vseap1 being a key interacting partner.
  • Vseap1 expression and its associated transcripts are linked to v-src activity and cellular resistance to oxidative stress.
  • These findings contribute to understanding the molecular mechanisms of RSV-induced transformation and metastasis.

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