The dimerization property of glutathione S-transferase partially reactivates Bcr-Abl lacking the oligomerization domain.

@article{Maru1996TheDP,
  title={The dimerization property of glutathione S-transferase partially reactivates Bcr-Abl lacking the oligomerization domain.},
  author={Yoshiro Maru and Daniel E.H Afar and Owen N Witte and Masabumi Shibuya},
  journal={The Journal of biological chemistry},
  year={1996},
  volume={271 26},
  pages={15353-7}
}
Bcr-Abl oncoproteins are responsible for the pathogenesis of human leukemias with a reciprocal chromosome translocation t(9;22). The amino-terminal Bcr sequence has a potential to form a homotetramer (tetramer domain), and destructions of the tetramer domain cause a complete loss of biological activities in Bcr-Abl. Here we show that Bcr-Abl in which the tetramer domain is replaced with glutathione S-transferase (GST) with a dimerizing ability (GST/Bcr-Abl-(Delta1-160)) can no longer induce an… CONTINUE READING
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