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

Citation
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
Citations number
43
Categorie Soggetti
Entomology/Pest Control","Biochemistry & Biophysics
Journal title
ARCHIVES OF INSECT BIOCHEMISTRY AND PHYSIOLOGY
ISSN journal
07394462 → ACNP
Volume
45
Issue
3
Year of publication
2000
Pages
109 - 116
Database
ISI
SICI code
0739-4462(200011)45:3<109:COT1VP>2.0.ZU;2-G
Abstract
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.