BAIT

SIS1

type II HSP40 co-chaperone SIS1, L000001898, YNL007C
Type II HSP40 co-chaperone that interacts with the HSP70 protein Ssa1p; shuttles between cytosol and nucleus; mediates delivery of misfolded proteins into the nucleus for degradation; involved in proteasomal degradation of misfolded cytosolic proteins; protein abundance increases in response to DNA replication stress; polyQ aggregates sequester Sis1p and interfere with clearance of misfolded proteins; similar to bacterial DnaJ proteins and mammalian DnaJB1
GO Process (4)
GO Function (1)
GO Component (2)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Saccharomyces cerevisiae (S288c)
PREY

TSA1

TPX1, ZRG14, thioredoxin peroxidase TSA1, cTPxI, L000002365, YML028W
Thioredoxin peroxidase; acts as both ribosome-associated and free cytoplasmic antioxidant; self-associates to form high-molecular weight chaperone complex under oxidative stress; chaperone activity essential for growth in zinc deficiency; required for telomere length maintenance; protein abundance increases, forms cytoplasmic foci during DNA replication stress; TSA1 has a paralog, TSA2, that arose from the whole genome duplication
Saccharomyces cerevisiae (S288c)

Affinity Capture-MS

An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods.

Publication

Subcellular localization of the J-protein Sis1 regulates the heat shock response.

Feder ZA, Ali A, Singh A, Krakowiak J, Zheng X, Bindokas VP, Wolfgeher D, Kron SJ, Pincus D

Cells exposed to heat shock induce a conserved gene expression program, the heat shock response (HSR), encoding protein homeostasis (proteostasis) factors. Heat shock also triggers proteostasis factors to form subcellular quality control bodies, but the relationship between these spatial structures and the HSR is unclear. Here we show that localization of the J-protein Sis1, a cofactor for the chaperone Hsp70, ... [more]

J Cell Biol Jan. 04, 2021; 220(1); [Pubmed: 33326013]

Throughput

  • High Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
TSA1 SIS1
Affinity Capture-MS
Affinity Capture-MS

An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods.

High2BioGRID
3610027
SIS1 TSA1
Proximity Label-MS
Proximity Label-MS

An interaction is inferred when a bait-enzyme fusion protein selectively modifies a vicinal protein with a diffusible reactive product, followed by affinity capture of the modified protein and identification by mass spectrometric methods.

High-BioGRID
3658326

Curated By

  • BioGRID