Sp. Holmes et al., Cloning of the 16-kDa V-ATPase proteolipid subunit from the red imported fire ant Solenopsis invicta buren (Hymenoptera : formicidae), ARCH INS B, 45(3), 2000, pp. 109-116
V-ATPases are ubiquitous proton pumps found in eukaryotes, and are importan
t in regulating the pH of cell compartments and in creating membrane potent
ials, The V-ATPase creates a proton gradient that is used as an energy sour
ce for the transport of other ions. The 16-kDa proteolipid is the proton-tr
anslocating subunit c of V-ATPases. Using PCR methods, we have cloned the f
ire ant 16-kDa subunit c, providing the first molecular characterization of
this protein in a social insect. Northern blot analysis revealed three pos
sible different transcripts. The presence of V-ATPases in ant Malpighian tu
bules had been previously demonstrated, where they provide the proton gradi
ent necessary for the excretion of other ions and the formation of primary
urine, The 16-kDa proteolipid is highly conserved among insects, and in ant
s may be important to the critical processes of diuresis and olfaction as a
key component of the V-ATPase. (C) 2001 Wiley-Liss, Inc.