ABSTRACT

The eukaryotic V-ATPases function as proton pumps that are

involved in the acidification of cellular compartments such as the

Golgi apparatus or lysosomes. In addition, some prokaryotes, such as

the Thermus thermophilus or Enterococcus hirae, contain a member of the family (or homologue) of the V-ATPases in their membranes.

The prokaryotic V-type ATPases/synthases (prokaryotic V-ATPases)

have simpler subunit compositions than eukaryotic V-ATPases

and, thus, are useful subjects for studying chemical, physical, and

structural properties of V-ATPase. In this review, we focus on the

results of recent studies on the structure of the V-ATPase from the

eubacteria, both T. thermophilus and E. hirae.