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

被引:0
作者
Holmes, SP [1 ]
Frazier, SK [1 ]
Pietrantonio, PV [1 ]
机构
[1] Texas A&M Univ, Dept Entomol, College Stn, TX 77843 USA
关键词
insect; vacuolar proton ATPase; ductin; proton channel; subunit c;
D O I
10.1002/1520-6327(200011)45:3<109::AID-ARCH2>3.0.CO;2-X
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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. (C) 2001 Wiley-Liss, Inc.
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页码:109 / 116
页数:8
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