Brief Communication abstract
Nature Cell Biology 3, 939 - 943 (2001)
Published online: 13 September 2001 | doi:10.1038/ncb1001-939
Proteins containing the UBA domain are able to bind to multi-ubiquitin chains
Caroline R.M. Wilkinson1,2, Michael Seeger1, Rasmus Hartmann-Petersen1, Miranda Stone1, Mairi Wallace1, Colin Semple1 & Colin Gordon1
The UBA domain is a motif found in a variety of proteins, some of which are associated with the ubiquitin–proteasome system1, 2. We describe the isolation of a fission-yeast gene, mud1+, which encodes a UBA domain containing protein that is able to bind multi-ubiquitin chains. We show that the UBA domain is responsible for this activity. Two other proteins containing this motif, the fission-yeast homologues of Rad23 and Dsk2, are also shown to bind multi-ubiquitin chains via their UBA domains. These two proteins are implicated, along with the fission-yeast Pus1(S5a/Rpn10) subunit of the 26 S proteasome, in the recognition and turnover of substrates by this proteolytic complex.
- MRC Human Genetics Unit, Western General Hospital, Crewe Road, Edinburgh EH4 2XU, UK
- Present address: Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston Massachusetts 02115, USA
Correspondence to: Colin Gordon1 e-mail: colin.gordon@hgu.mrc.ac.uk
