Cloning of the 16-kDa V-ATPase proteolipid subunit from the red imported fire ant Solenopsis invicta buren (Hymenoptera: Formicidae).

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.

authors

Holmes SP,Frazier SK,Pietrantonio PV

doi

10.1002/1520-6327(200011)45:3<109::AID-ARCH2>3.0.C

subject

Has Abstract

pub_date

2000-11-01 00:00:00

pages

109-16

issue

3

eissn

0739-4462

issn

1520-6327

pii

10.1002/1520-6327(200011)45:3<109::AID-ARCH2>3.0.C

journal_volume

45

pub_type

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