Structural comparison of the vacuolar and Golgi V-ATPases from Saccharomyces cerevisiae
| Autor: | Stephanie A. Bueler, Thamiya Vasanthakumar, Di Wu, Victoria Beilsten-Edmands, Carol V. Robinson, John L. Rubinstein |
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| Rok vydání: | 2019 |
| Předmět: |
0303 health sciences
Multidisciplinary biology Endosome Chemistry ATPase Protein subunit Saccharomyces cerevisiae Vacuole Golgi apparatus biology.organism_classification 03 medical and health sciences symbols.namesake 0302 clinical medicine Biochemistry biology.protein symbols V-ATPase Protein maturation 030217 neurology & neurosurgery 030304 developmental biology |
| Zdroj: | Proceedings of the National Academy of Sciences. 116:7272-7277 |
| ISSN: | 1091-6490 0027-8424 |
| DOI: | 10.1073/pnas.1814818116 |
| Popis: | Proton-translocating vacuolar-type ATPases (V-ATPases) are necessary for numerous processes in eukaryotic cells, including receptor-mediated endocytosis, protein maturation, and lysosomal acidification. In mammals, V-ATPase subunit isoforms are differentially targeted to various intracellular compartments or tissues, but how these subunit isoforms influence enzyme activity is not clear. In the yeast Saccharomyces cerevisiae , isoform diversity is limited to two different versions of the proton-translocating subunit a: Vph1p, which is targeted to the vacuole, and Stv1p, which is targeted to the Golgi apparatus and endosomes. We show that purified V-ATPase complexes containing Vph1p have higher ATPase activity than complexes containing Stv1p and that the relative difference in activity depends on the presence of lipids. We also show that V O complexes containing Stv1p could be readily purified without attached V 1 regions. We used this effect to determine structures of the membrane-embedded V O region with Stv1p at 3.1-Å resolution, which we compare with a structure of the V O region with Vph1p that we determine to 3.2-Å resolution. These maps reveal differences in the surface charge near the cytoplasmic proton half-channel. Both maps also show the presence of bound lipids, as well as regularly spaced densities that may correspond to ergosterol or bound detergent, around the c-ring. |
| Databáze: | OpenAIRE |
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