Abstract
ABSTRACT The subunit structure of the vacuolar H+-ATPase (V-ATPase) membrane sector is not entirely known. The proteolipid is the only subunit that has been implicated in the mechanism of energy transfer in the enzyme. We have identified a protein (M16) that co-purifies with the V-ATPase complex from bovine chromaffin granules. Information obtained from the amino acid sequence of a proteolytic fragment of M16 was used to clone a bovine adrenal cDNA encoding this protein. The cDNA encodes a hydrophilic protein of 118 amino acid residues with a calculated molecular mass of 13 682 Da. Amino acid sequence analysis revealed that M16 exhibits a significant homology to subunit b of F-ATPases. M16 is smaller than subunit b and contains no apparent transmembrane segment in its N terminus. The remainder of subunit b is related to M16 not only by its amino acid sequence but also in its predicted structure of helix–turn–helix. The structural and evolutionary implications of these findings are discussed.
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Dates
Type | When |
---|---|
Created | 4 years, 4 months ago (April 25, 2021, 12:03 a.m.) |
Deposited | 1 year, 5 months ago (March 17, 2024, 5:32 p.m.) |
Indexed | 3 weeks, 3 days ago (Aug. 6, 2025, 8:27 a.m.) |
Issued | 29 years, 3 months ago (May 1, 1996) |
Published | 29 years, 3 months ago (May 1, 1996) |
Published Online | 29 years, 3 months ago (May 1, 1996) |
Published Print | 29 years, 3 months ago (May 1, 1996) |
@article{Supekova_1996, title={A Novel Subunit of Vacuolar H+-ATPase Related to The b Subunit of F-ATPases}, volume={199}, ISSN={1477-9145}, url={http://dx.doi.org/10.1242/jeb.199.5.1147}, DOI={10.1242/jeb.199.5.1147}, number={5}, journal={Journal of Experimental Biology}, publisher={The Company of Biologists}, author={Supekova, Lubica and Sbia, Mohammed and Supek, Frantisek and Ma, Yuemei and Nelson, Nathan}, year={1996}, month=may, pages={1147–1156} }