The V0V1-ATPase of @entity4691 catalyzes @entity855 synthesis coupled with proton translocation. It consists of an ATPase-active V1 part (ABDF) and a proton channel V0 part (CLEGI), but the arrangement of each subunit is still largely unknown. Here we found that acid treatment of V0V1-ATPase induced its dissociation into two subcomplexes, one with subunit composition ABDFCL and the other with EGI. Exposure of the isolated V0 to acid or 8 m @entity1133 also produced two subcomplexes, EGI and CL. Thus, the C subunit (homologue of d subunit, @entity375 @entity58890 ) associates with the L subunit ring tightly, and I (homologue of 100-kDa subunit, @entity375 @entity11858 ), E, and G subunits constitute a stable complex. Based on these observations and our recent demonstration that D, F, and L subunits rotate relative to A3B3 (Imamura, H., Nakano, M., Noji, H., Muneyuki, E., Ohkuma, S., Yoshida, M., and Yokoyama, K. (2003) Proc. Natl. Acad. Sci. U. S. A. 100, 2312-2315; Yokoyama, K., Nakano, M., Imamura, H., Yoshida, M., and Tamakoshi, M. (2003) J. Biol. Chem. 278, 24255-24258), we propose that C, D, F, and L subunits constitute the central rotor shaft and A, B, E, G, and I subunits comprise the surrounding stator apparatus in the V0V1-ATPase.

Subunit arrangement in V-ATPase from XXXX .

@entity4691 :: ('274', 'Species') :: ['Thermus thermophilus'] @entity1133 :: ('MESH:D014508', 'Chemical') :: ['urea'] @entity58890 :: ('851168(Tax:4932)', 'Gene') :: ['Vma6p'] @entity11858 :: ('854444(Tax:4932)', 'Gene') :: ['Vph1p'] @entity375 :: ('4932', 'Species') :: ['yeast'] @entity855 :: ('MESH:D000255', 'Chemical') :: ['ATP']
@entity4691 :: (274,Species) :: ['Thermus thermophilus']
