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- Title
Dimer formation of subunit G of the yeast V-ATPase
- Authors
Armbrüster, Andrea; Bailer, Susanne M.; Koch, Michel H.J.; Godovac-Zimmermann, Jasminka; Grüber, Gerhard
- Abstract
The G subunit of the vacuolar ATPase (V-ATPase) is a component of the stalk connecting the V1 and VO sectors of the enzyme and is essential for normal assembly and function. Subunit G (Vma10p) of the yeast V-ATPase was expressed in Escherichia coli as a soluble protein and was purified to homogeneity. The molecular mass of subunit G, determined by Native-polyacrylamide gel electrophoresis, gel filtration analysis and small-angle X-ray scattering, was approximately 28±2 kDa, indicating that this protein is dimeric. With a radius of gyration (Rg) and a maximum size (Dmax) of 2.7±0.2 nm and 8.0±0.3 nm, respectively, the G-dimer is rather elongated. To understand which region of subunit G is required to mediate dimerization, a G38–144 form (the carboxyl-terminus) was expressed and purified. G38–144 is homogeneous, with a molecular mass of approximately 12±3 kDa, indicating a monomeric form in solution.
- Subjects
ADENOSINE triphosphatase; ESCHERICHIA coli
- Publication
FEBS Letters, 2003, Vol 546, Issue 2/3, p395
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/S0014-5793(03)00643-4