Format

Send to

Choose Destination
Biochemistry. 2015 Jul 28;54(29):4423-6. doi: 10.1021/acs.biochem.5b00504. Epub 2015 Jul 17.

Prb1 Protease Activity Is Required for Its Recognition by the F-Box Protein Saf1.

Author information

1
†Department of Biochemistry and Biophysics, University of California, San Francisco, California 94158, United States.
2
‡Department of Cellular and Molecular Pharmacology, University of California, San Francisco, California 94158, United States.

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.

PMID:
26161950
PMCID:
PMC4816488
DOI:
10.1021/acs.biochem.5b00504
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for American Chemical Society Icon for PubMed Central
Loading ...
Support Center