Palmitoylation of the Rous sarcoma virus transmembrane glycoprotein is required for protein stability and virus infectivity.

@article{OchsenbauerJambor2001PalmitoylationOT,
  title={Palmitoylation of the Rous sarcoma virus transmembrane glycoprotein is required for protein stability and virus infectivity.},
  author={Christina Ochsenbauer-Jambor and David C Miller and Charles R Roberts and Sung S Rhee and Eric Hunter},
  journal={Journal of virology},
  year={2001},
  volume={75 23},
  pages={11544-54}
}
The Rous sarcoma virus (RSV) transmembrane (TM) glycoprotein is modified by the addition of palmitic acid. To identify whether conserved cysteines within the hydrophobic anchor region are the site(s) of palmitoylation, and to determine the role of acylation in glycoprotein function, cysteines at residues 164 and 167 of the TM protein were mutated to glycine (C164G, C167G, and C164G/C167G). In CV-1 cells, palmitate was added to env gene products containing single mutations but was absent in the… CONTINUE READING

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