A deubiquitinating enzyme interacts with SIR4 and regulates silencing in S. cerevisiae.

Abstract:

:The SIR2, SIR3, and SIR4 proteins are required for silencing of transcription at the silent mating type loci and at telomeres in yeast. Using protein affinity chromatography, we show that SIR2, SIR3, and two proteins of 69 and 110 kDa tightly associate with SIR4. Surprisingly, the 110 kDa SIR4-binding protein is identical to UBP3, one of several previously described yeast enzymes that deubiquitinate target proteins. Deletion of the UBP3 gene results in markedly improved silencing of genes inserted either near a telomere or at one of the silent mating type loci, indicating that UBP3 is an inhibitor of silencing. We discuss possible roles for UBP3 in controlling the activity or assembly of the SIR protein complex.

journal_name

Cell

journal_title

Cell

authors

Moazed D,Johnson D

doi

10.1016/s0092-8674(00)80139-7

subject

Has Abstract

pub_date

1996-08-23 00:00:00

pages

667-77

issue

4

eissn

0092-8674

issn

1097-4172

pii

S0092-8674(00)80139-7

journal_volume

86

pub_type

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