Chlorella virus MT325 encodes water and potassium channels that interact synergistically

被引:40
作者
Gazzarrini, S
Kang, M
Epimashko, S
Van Etten, JL
Dainty, J
Thiel, G
Moroni, A
机构
[1] Univ Nebraska, Dept Plant Pathol, Lincoln, NE 68583 USA
[2] Univ Nebraska, Nebraska Ctr Virol, Lincoln, NE 68583 USA
[3] Univ Milan, Consiglio Nazl Ric, Dipartimento Biol, I-20133 Milan, Italy
[4] Univ Milan, Consiglio Nazl Ric, Ist Biofis, I-20133 Milan, Italy
[5] Univ Toronto, Dept Bot, Toronto, ON M5S 3B2, Canada
[6] Tech Univ Darmstadt, Inst Bot, D-64287 Darmstadt, Germany
[7] Univ Milan, Ist Nazl Fis Mat, I-20133 Milan, Italy
关键词
water transport; aquaglyceroporins; membrane potential; osmoregulation; viroporin;
D O I
10.1073/pnas.0600848103
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Fast and selective transport of water through cell membranes is facilitated by water channels. Water channels belonging to the major intrinsic proteins (MIPS) family have been found in all three domains of life,Archaea, Bacteria, and Eukarya. Here we show that Chlorella virus MT325 has a water channel gene, aqpv1, that forms a functional aquaglyceroporin in oocytes. aqpv1 is transcribed during infection together with MT325 kcv, a gene encoding a previously undescribed type of viral potassium channel. Coexpression of AQPV1 and MT325-Kcv in Xenopus oocytes synergistically increases water transport, suggesting a possible concerted action of the two channels in the infection cycle. The two channels operate by a thermodynamically coupled mechanism that simultaneously alters water conductance and driving force for water movement. Considering the universal role of osmosis, this mechanism is relevant to any cell coexpressing water and potassium channels and could have pathological as well as basic physiological relevance.
引用
收藏
页码:5355 / 5360
页数:6
相关论文
共 32 条
[1]   HYPOTONICITY ACTIVATES A NATIVE CHLORIDE CURRENT IN XENOPUS-OOCYTES [J].
ACKERMAN, MJ ;
WICKMAN, KD ;
CLAPHAM, DE .
JOURNAL OF GENERAL PHYSIOLOGY, 1994, 103 (02) :153-179
[2]  
ACKERMAN MJ, 1994, JPN J PHYSIOL, V44, pS17
[3]   The aquaporins, blueprints for cellular plumbing systems [J].
Agre, P ;
Bonhivers, M ;
Borgnia, MJ .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (24) :14659-14662
[4]   Cellular and molecular biology of the aquaporin water channels [J].
Borgnia, M ;
Nielsen, S ;
Engel, A ;
Agre, P .
ANNUAL REVIEW OF BIOCHEMISTRY, 1999, 68 :425-458
[5]   A novel potassium channel encoded by Ectocarpus siliculosus virus [J].
Chen, J ;
Cassar, SC ;
Zhang, D ;
Gopalakrishnan, M .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2005, 326 (04) :887-893
[6]   Three-dimensional organization of a human water channel [J].
Cheng, AC ;
vanHoek, AN ;
Yeager, M ;
Verkman, AS ;
Mitra, AK .
NATURE, 1997, 387 (6633) :627-630
[7]   Prediction of functional residues in water channels and related proteins [J].
Froger, A ;
Tallur, B ;
Thomas, D ;
Delamarche, C .
PROTEIN SCIENCE, 1998, 7 (06) :1458-1468
[8]   Structure of a glycerol-conducting channel and the basis for its selectivity [J].
Fu, DX ;
Libson, A ;
Miercke, LJW ;
Weitzman, C ;
Nollert, P ;
Krucinski, J ;
Stroud, RM .
SCIENCE, 2000, 290 (5491) :481-486
[9]   Long distance interactions within the potassium channel pore are revealed by molecular diversity of viral proteins [J].
Gazzarrini, S ;
Kang, M ;
Van Etten, JL ;
Tayefeh, S ;
Kast, SM ;
DiFrancesco, D ;
Thiel, G ;
Moroni, A .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (27) :28443-28449
[10]   Viroporins [J].
Gonzalez, ME ;
Carrasco, L .
FEBS LETTERS, 2003, 552 (01) :28-34