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  • 标题:An exchanger-like protein underlies the large Mg2+ current in Paramecium
  • 本地全文:下载
  • 作者:W. John Haynes ; Ching Kung ; Yoshiro Saimi
  • 期刊名称:Proceedings of the National Academy of Sciences
  • 印刷版ISSN:0027-8424
  • 电子版ISSN:1091-6490
  • 出版年度:2002
  • 卷号:99
  • 期号:24
  • 页码:15717-15722
  • DOI:10.1073/pnas.242603999
  • 语种:English
  • 出版社:The National Academy of Sciences of the United States of America
  • 摘要:There are very few molecules known to transport Mg2+ in eukaryotes. The membrane of Paramecium tetraurelia passes a large Mg2+-selective current and exhibits a corresponding backward swimming behavior. Both are missing in a group of mutants called eccentric. By sorting an indexed WT genomic library through microinjection into the macronucleus, we have isolated a DNA fragment that complements the eccentric mutations. The Mg2+ currents and behavior are restored fully in the transformed cells. Surprisingly, the conceptually translated protein is not homologous to any known ion channel but instead has some similarity to K+-dependent Na+/Ca2+ exchangers. Exchangers are either electrically silent or only pass very small and slow currents compared with ion-channel currents. In light of recent ion-channel crystal structures and considering the need to have narrow ion-selective filters, we speculate on how an exchanger might evolve to show channel-like activities in special circumstances. The significance of finding the molecular basis of a Mg2+-specific pathway is also discussed.
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