| Autor: |
Vasanthakumar, Thamiya, Keon, Kristine A., Bueler, Stephanie A., Jaskolka, Michael C., Rubinstein, John L. |
| Zdroj: |
Nature Structural and Molecular Biology; 20220101, Issue: Preprints p1-10, 10p |
| Abstrakt: |
Vacuolar-type ATPases (V-ATPases) are rotary enzymes that acidify intracellular compartments in eukaryotic cells. These multi-subunit complexes consist of a cytoplasmic V1region that hydrolyzes ATP and a membrane-embedded VOregion that transports protons. V-ATPase activity is regulated by reversible dissociation of the two regions, with the isolated V1and VOcomplexes becoming autoinhibited on disassembly and subunit C subsequently detaching from V1. In yeast, assembly of the V1and VOregions is mediated by the regulator of the ATPase of vacuoles and endosomes (RAVE) complex through an unknown mechanism. We used cryogenic-electron microscopy of yeast V-ATPase to determine structures of the intact enzyme, the dissociated but complete V1complex and the V1complex lacking subunit C. On separation, V1undergoes a dramatic conformational rearrangement, with its rotational state becoming incompatible for reassembly with VO. Loss of subunit C allows V1to match the rotational state of VO, suggesting how RAVE could reassemble V1and VOby recruiting subunit C. |
| Databáze: |
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