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  • Title: Cloning of the 16-kDa V-ATPase proteolipid subunit from the red imported fire ant Solenopsis invicta buren (Hymenoptera: Formicidae).
    Author: Holmes SP, Frazier SK, Pietrantonio PV.
    Journal: Arch Insect Biochem Physiol; 2000 Nov; 45(3):109-16. PubMed ID: 11169750.
    Abstract:
    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.
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