Abstract:
:The SCF ubiquitin ligase associates with substrates through its F-box protein adaptor. Substrates are typically recognized through a defined phosphodegron. Here, we characterize the interaction of the F-box protein Saf1 with Prb1, one of its vacuolar protease substrates. We show that Saf1 binds the mature protein but ubiquitinates only the zymogen precursor. The ubiquitinated lysine was found to be in a peptide eliminated from the mature protein. Mutations that eliminate the catalytic activity of Prb1, or the related substrate Prc1, block Saf1 targeting of the zymogen precursor. Our data suggest that Saf1 does not require a conventional degron as do other F-box proteins but instead recognizes the catalytic site itself.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Mark KG,Meza-Gutierrez F,Johnson JR,Newton BW,Krogan NJ,Toczyski DPdoi
10.1021/acs.biochem.5b00504subject
Has Abstractpub_date
2015-07-28 00:00:00pages
4423-6issue
29eissn
0006-2960issn
1520-4995journal_volume
54pub_type
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