K29-Selective Ubiquitin Binding Domain Reveals Structural Basis of Specificity and Heterotypic Nature of K29 Polyubiquitin

@inproceedings{Kristariyanto2015K29SelectiveUB,
  title={K29-Selective Ubiquitin Binding Domain Reveals Structural Basis of Specificity and Heterotypic Nature of K29 Polyubiquitin},
  author={Yosua Adi Kristariyanto and Syed Arif Abdul Rehman and David G Campbell and Nicholas A. Morrice and Clare A Johnson and Rachel Toth and Yogesh Kulathu},
  booktitle={Molecular cell},
  year={2015}
}
Polyubiquitin chains regulate diverse cellular processes through the ability of ubiquitin to form chains of eight different linkage types. Although detected in yeast and mammals, little is known about K29-linked polyubiquitin. Here we report the generation of K29 chains in vitro using a ubiquitin chain-editing complex consisting of the HECT E3 ligase UBE3C and the deubiquitinase vOTU. We determined the crystal structure of K29-linked diubiquitin, which adopts an extended conformation with the… CONTINUE READING