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

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

Biochemistry

journal_title

Biochemistry

authors

Mark KG,Meza-Gutierrez F,Johnson JR,Newton BW,Krogan NJ,Toczyski DP

doi

10.1021/acs.biochem.5b00504

subject

Has Abstract

pub_date

2015-07-28 00:00:00

pages

4423-6

issue

29

eissn

0006-2960

issn

1520-4995

journal_volume

54

pub_type

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