The tail of a ubiquitin-conjugating enzyme redirects multi-ubiquitin chain synthesis from the lysine 48-linked configuration to a novel nonlysine-linked form.

@article{Hodgins1996TheTO,
  title={The tail of a ubiquitin-conjugating enzyme redirects multi-ubiquitin chain synthesis from the lysine 48-linked configuration to a novel nonlysine-linked form.},
  author={Raibert Hodgins and C S Gwozd and Terra G Arnason and Margaret Cummings and Michael J. Ellison},
  journal={The Journal of biological chemistry},
  year={1996},
  volume={271 46},
  pages={28766-71}
}
The UBC1 ubiquitin-conjugating enzyme from Saccharomyces cerevisiae has an overlapping function with the UBC4 and UBC5 enzymes in the yeast stress response and an important role in the G0 to G1 transition that accompanies spore germination (Seufert, W., McGrath, J. P., and Jentsch, S. (1990) EMBO J. 9, 4573-4541). In the present work we report that the UBC1 enzyme assembles onto itself a multi-ubiquitin chain in vitro whose linkage configuration is dependent on the unconserved carboxyl-terminal… CONTINUE READING

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