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

详细信息    查看全文

• 作者：Kevin G. Mark ; Fernando Meza-Gutierrez ; Jeffrey R. Johnson ; Billy W. Newton ; Nevan J. Krogan ; David P. Toczyski
• 刊名：Biochemistry
• 出版年：2015
• 出版时间：July 28, 2015
• 年：2015
• 卷：54
• 期：29
• 页码：4423-4426
• 全文大小：229K
• ISSN：1520-4995

文摘

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.