Premium
Cloning of the 16‐kDa V‐ATPase proteolipid subunit from the red imported fire ant Solenopsis invicta buren (Hymenoptera: Formicidae)
Author(s) -
Holmes Steven Paul,
Frazier Sam Kiah,
Pietrantonio Patricia Victoria
Publication year - 2000
Publication title -
archives of insect biochemistry and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.576
H-Index - 66
eISSN - 1520-6327
pISSN - 0739-4462
DOI - 10.1002/1520-6327(200011)45:3<109::aid-arch2>3.0.co;2-x
Subject(s) - biology , protein subunit , malpighian tubule system , atpase , proton transport , biochemistry , gene , botany , enzyme , membrane , larva , midgut
V‐ATPases are ubiquitous proton pumps found in eukaryotes, and are important in regulating the pH of cell compartments and in creating membrane potentials. The V‐ATPase creates a proton gradient that is used as an energy source for the transport of other ions. The 16‐kDa proteolipid is the proton‐translocating subunit c of V‐ATPases. Using PCR methods, we have cloned the fire ant 16‐kDa subunit c, providing the first molecular characterization of this protein in a social insect. Northern blot analysis revealed three possible different transcripts. The presence of V‐ATPases in ant Malpighian tubules had been previously demonstrated, where they provide the proton gradient necessary for the excretion of other ions and the formation of primary urine. The 16‐kDa proteolipid is highly conserved among insects, and in ants may be important to the critical processes of diuresis and olfaction as a key component of the V‐ATPase. Arch. Insect Biochem. Physiol. 45:109–116, 2000. © 2001 Wiley‐Liss, Inc.