Abstract:
:Ataxin-3, which is encoded by a gene that has been associated with Machado-Joseph disease, contains a catalytic N-terminal Josephin domain with deubiquitinase activity. Here, we show that the Josephin domain of ataxin 3 catalyzes endo-type cleavage of Lys48-linked polyubiquitin. Furthermore, NMR data obtained following site-specific paramagnetic spin labeling of Lys48-linked di-ubiquitin revealed that both ubiquitin units interact with the Josephin domain, with the C-terminal Gly76 of the proximal unit being situated in the vicinity of the catalytic triad of Josephin domain. Our results help to elucidate how the substrate is recognized by the Josephin domain and properly positioned for an endo-type deubiquitination reaction.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Satoh T,Sumiyoshi A,Yagi-Utsumi M,Sakata E,Sasakawa H,Kurimoto E,Yamaguchi Y,Li W,Joazeiro CA,Hirokawa T,Kato Kdoi
10.1016/j.febslet.2014.10.013subject
Has Abstractpub_date
2014-11-28 00:00:00pages
4422-30issue
23eissn
0014-5793issn
1873-3468pii
S0014-5793(14)00748-0journal_volume
588pub_type
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