Proteomics

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Sir4 H-BRCT domain interacts with multiple phospho-proteins to regulate heterochromatic repression


ABSTRACT: In Saccharomyces cerevisiae, the Silent Information Regulator (SIR) proteins Sir2/3/4 form a complex suppressing transcription of genes at subtelomeric regions and the homothallic mating type (HM) loci. Here we identify a non-canonical BRCA1 C-terminal domain (H-BRCT) in Sir4 which is responsible for tethering telomeres to the nuclear periphery. We show that Sir4 H-BRCT and the closely related Dbf4 H-BRCT serve as selective phospho-epitope recognition domains that bind to a variety of phosphorylated target peptides. We present detailed structural information about the binding mode of established Sir4 interactors (Esc1, Ty5, Ubp10) and identify several novel interactors of Sir4 H-BRCT, including the E3 ubiquitin ligase Tom1. Based on these findings, we propose a phospho-peptide consensus motif for interaction with Sir4 H-BRCT and Dbf4 H-BRCT. Ablation of the Sir4 H-BRCT phospho-peptide interaction disrupts SIR-mediated repression and perinuclear localization. In conclusion, the Sir4 H-BRCT domain serves as a hub for recruitment of phosphorylated target proteins to heterochromatin to properly regulate silencing and nuclear order.

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)

SUBMITTER: Vytautas Iesmantavicius  

LAB HEAD: Heinz Gut

PROVIDER: PXD014119 | Pride | 2019-09-13

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
1452_mqpar.xml Xml
F1_170616_Vyt_1452_R1.raw Raw
F1_170616_Vyt_1452_R2.raw Raw
F1_170616_Vyt_1452_R3.raw Raw
F1_170616_Vyt_1452_W1.raw Raw
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Publications

The Sir4 H-BRCT domain interacts with phospho-proteins to sequester and repress yeast heterochromatin.

Deshpande Ishan I   Keusch Jeremy J JJ   Challa Kiran K   Iesmantavicius Vytautas V   Gasser Susan M SM   Gut Heinz H  

The EMBO journal 20190912 20


In Saccharomyces cerevisiae, the silent information regulator (SIR) proteins Sir2/3/4 form a complex that suppresses transcription in subtelomeric regions and at the homothallic mating-type (HM) loci. Here, we identify a non-canonical BRCA1 C-terminal domain (H-BRCT) in Sir4, which is responsible for tethering telomeres to the nuclear periphery. We show that Sir4 H-BRCT and the closely related Dbf4 H-BRCT serve as selective phospho-epitope recognition domains that bind to a variety of phosphoryl  ...[more]

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