BAIT

VMA10

YHR039C-B, H(+)-transporting V1 sector ATPase subunit G, YHR039BC, L000002954, YHR039C-A
Subunit G of the V1 peripheral membrane domain of V-ATPase; part of the electrogenic proton pump found throughout the endomembrane system; involved in vacuolar acidification; the V1 peripheral membrane domain of the vacuolar H+-ATPase (V-ATPase) has eight subunits
GO Process (1)
GO Function (1)
GO Component (2)
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

Oxidative stress protein Oxr1 promotes V-ATPase holoenzyme disassembly in catalytic activity-independent manner.

Khan MM, Lee S, Couoh-Cardel S, Oot RA, Kim H, Wilkens S, Roh SH

The vacuolar ATPase (V-ATPase) is a rotary motor proton pump that is regulated by an assembly equilibrium between active holoenzyme and autoinhibited V1 -ATPase and Vo proton channel subcomplexes. Here, we report cryo-EM structures of yeast V-ATPase assembled in vitro from lipid nanodisc reconstituted Vo and mutant V1 . Our analysis identified holoenzymes in three active rotary states, indicating that binding ... [more]

EMBO J Feb. 01, 2022; 41(3);e109360 [Pubmed: 34918374]

Throughput

  • High Throughput

Curated By

  • BioGRID