The progenitor of ATP synthases was closely related to the current vacuolar H+‐ATPase

FEBS Letters

Nelson, Nathan¹  Nelson, Hannah¹ 

[1] Roche Institute of Molecular Biology, Roche Research Center, Nutley, NJ 07110, USA

关键词: ATPase;    vacuolar H+-;    ATP synthase;    Proteolipid;    Evolution;    F-ATPase;    the eubacterial type H+-ATPase (F0F1);    V-ATPase;    vacuolar type H+-ATPase;    DCCD;    N;    N′-dycyclohexylcarbodiimide;   

DOI  :  10.1016/0014-5793(89)81259-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The gene encoding the proteolipid of the vacuolar H⁺-ATPase of yeast was cloned and sequenced. The deduced amino acid sequence of the yeast protein is highly homologous to that of the proteolipid from bovine chromaffin granules. In contrast to other membrane proteins the transmembrane segments of the bovine and yeast proteolipids were much more conserved than the hydrophilic parts. The fourth transmembrane segment, which contains the DCCD-binding site, was conserved 100%. Comparison of vacuolar and eubacterial proteolipids revealed a homology which pointed to a common ancestral gene that underwent gene duplication to form the vacuolar proteolipids. Additional support for this notion came from the amino acid sequences of subunits involved in the catalytic sectors of archaebacterial ATP synthase and plant and yeast vacuolar H⁺-ATPases, which reveal extensive sequence homology. Slight, but significant, homology between the archaebacterial and eubacterial ATP synthases was observed. These observations might suggest that the progenitor of ATP synthases was closely related to the present vacuolar H⁺-ATPases.

【 授权许可】

Unknown