help button home button Biophys. J.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Picco, C.
Right arrow Articles by Gambale, F.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Picco, C.
Right arrow Articles by Gambale, F.
Biophysical Journal 86:224-234 (2004)
© 2004 The Biophysical Society

Histidines Are Responsible for Zinc Potentiation of the Current in KDC1 Carrot Channels

Cristiana Picco *, Monica Bregante *, Alessia Naso *, Paola Gavazzo *, Alex Costa {dagger}, Elide Formentin {dagger}, Patrick Downey {dagger}, Fiorella Lo Schiavo {dagger} and Franco Gambale *

* Istituto di Biofisica, Consiglio Nazionale delle Ricerche, Sezione di Genova, Genova, Italy and {dagger} Dipartimento di Biologia, Universita' di Padova, Padova, Italy

Correspondence: Address reprint requests to Franco Gambale, Istituto di Biofisica, Via De Marini 6, 16149 Genova, Italy. Tel.: 39-010-647-5550; Fax: 39-010-647-5500; E-mail: gambale{at}area.ge.cnr.it.

Unlike all plant inward-rectifying potassium channels, the carrot channel KDC1 has two histidine pairs (H161,H162) in the S3–S4 and (H224,H225) in the S5–S6 linkers. When coinjected with KAT1 in Xenopus oocytes, KDC1 participates in the formation of heteromultimeric KDC1:KAT1 channels and the ionic current is potentiated by extracellular Zn2+. To investigate the potential interactions between KDC1 and zinc, a KDC1-KAT1 dimer was constructed. The dimeric and heteromeric channels displayed similar characteristics and the same sensitivity to zinc and other metals; this result suggests that zinc binding is mediated by residues in a single channel subunit. The KDC1:KAT1 currents were also potentiated by external Pb2+ and Cd2+ and inhibited by Ni2+. To investigate further the role of KDC1-histidines, these amino acids were mutated into alanines. The single mutations H225A, H161A, and H162A did not affect the response of the heteromeric channels to zinc. Conversely, the single mutant H224A and the double mutants (H224A,H225A) and (H161A,H162A) abolished zinc potentiation, but not that induced by Pb2+ or Cd2+. These results suggest that Zn2+ potentiation cannot be ascribed to simple electrostatic interactions between zinc and channel residues and that histidine 224 is crucial for zinc but not for lead potentiation of the current.




This article has been cited by other articles:


Home page
Biophys. JHome page
C. Picco, A. Naso, P. Soliani, and F. Gambale
The Zinc Binding Site of the Shaker Channel KDC1 from Daucus carota
Biophys. J., January 15, 2008; 94(2): 424 - 433.
[Abstract] [Full Text] [PDF]


Home page
Biophys. JHome page
A. Naso, R. Montisci, F. Gambale, and C. Picco
Stoichiometry Studies Reveal Functional Properties of KDC1 in Plant Shaker Potassium Channels
Biophys. J., November 15, 2006; 91(10): 3673 - 3683.
[Abstract] [Full Text] [PDF]


Home page
J Exp BotHome page
L. Yu, D. Becker, H. Levi, M. Moshelion, R. Hedrich, I. Lotan, A. Moran, U. Pick, L. Naveh, Y. Libal, et al.
Phosphorylation of SPICK2, an AKT2 channel homologue from Samanea motor cells
J. Exp. Bot., November 1, 2006; 57(14): 3583 - 3594.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2004 by the Biophysical Society.