A novel subunit of vacuolar H(+)-ATPase related to the b subunit of F-ATPases.
J Exp Biol
; 199(Pt 5): 1147-56, 1996 May.
Article
em En
| MEDLINE
| ID: mdl-8786335
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 13682Da. 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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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Vacúolos
/
ATPases Translocadoras de Prótons
/
ATPases Vacuolares Próton-Translocadoras
Tipo de estudo:
Prognostic_studies
Limite:
Animals
Idioma:
En
Revista:
J Exp Biol
Ano de publicação:
1996
Tipo de documento:
Article
País de afiliação:
Estados Unidos