HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Lagrée, V. Articles by Deschamps, S. Search for Related Content PubMed PubMed Citation Articles by Lagrée, V. Articles by Deschamps, S. Social Bookmarking                      What's this?

J Biol Chem, Vol. 273, Issue 20, 12422-12426, May 15, 1998

A Yeast Recombinant Aquaporin Mutant That Is Not Expressed or Mistargeted in Xenopus Oocyte Can Be Functionally Analyzed in Reconstituted Proteoliposomes

Valérie Lagrée, Isabelle Pellerin, Jean-François Hubert, Frédérique Tacnet^§, Françoise Le Cahérec, Nathalie Roudier^§, Daniel Thomas, Jean Gouranton, and Stéphane Deschamps

From the  UPRES-A CNRS, Biologie Cellulaire et Reproduction, Université de Rennes 1, 35042 Rennes cedex and ^§ Département de Biologie Cellulaire et Moléculaire, Service de Biologie Cellulaire, CEA-Saclay, 91191 Gif sur Yvette cedex, France

We have recently identified AQPcic (for aquaporin cicadella), an insect aquaporin found in the digestive tract of homopteran insects and involved in the elimination of water ingested in excess with the dietary sap (Le Cahérec, F., Deschamps, S., Delamarche, C., Pellerin, I., Bonnec, G., Guillam, M. T., Gouranton, J., Thomas, D., and Hubert, J. F. (1996) Eur. J. Biochem. 241, 707-715). Like many other aquaporins, AQPcic is inhibited by mercury reagents. In this study, we have demonstrated that residue Cys⁸² is essential for mercury inhibition. Another mutant version of AQPcic (AQP-C134S), expression of which in Xenopus laevis failed to produce an active molecule, was successfully expressed in Saccharomyces cerevisiae. Using stopped-flow analysis of reconstituted proteoliposomes, we demonstrated that the biological activity and Hg sensitivity of yeast-expressed wild type and mutant type AQPcic was readily assessed. Therefore, we propose that the yeast system is a valid alternative to Xenopus oocytes for studying particular mutants of aquaporin.

CiteULike

Complore

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				L. Duchesne, I. Pellerin, C. Delamarche, S. Deschamps, V. Lagree, A. Froger, G. Bonnec, D. Thomas, and J.-F. Hubert Role of C-terminal Domain and Transmembrane Helices 5 and 6 in Function and Quaternary Structure of Major Intrinsic Proteins. ANALYSIS OF AQUAPORIN/GLYCEROL FACILITATOR CHIMERIC PROTEINS J. Biol. Chem., May 31, 2002; 277(23): 20598 - 20604. [Abstract] [Full Text] [PDF]

				D. Fu, A. Libson, L. J. W. Miercke, C. Weitzman, P. Nollert, J. Krucinski, and R. M. Stroud Structure of a Glycerol-Conducting Channel and the Basis for Its Selectivity Science, October 20, 2000; 290(5491): 481 - 486. [Abstract] [Full Text]

				F. Sidoux-Walter, N. Lucien, R. Nissinen, P. Sistonen, S. Henry, J. Moulds, J.-P. Cartron, and P. Bailly Molecular heterogeneity of the Jknull phenotype: expression analysis of the Jk(S291P) mutation found in Finns Blood, August 15, 2000; 96(4): 1566 - 1573. [Abstract] [Full Text] [PDF]

				A. S. Verkman and A. K. Mitra Structure and function of aquaporin water channels Am J Physiol Renal Physiol, January 1, 2000; 278(1): F13 - F28. [Abstract] [Full Text] [PDF]

				I. Shinbo, K. Fushimi, M. Kasahara, K. Yamauchi, S. Sasaki, and F. Marumo Functional analysis of aquaporin-2 mutants associated with nephrogenic diabetes insipidus by yeast expression Am J Physiol Renal Physiol, November 1, 1999; 277(5): F734 - F741. [Abstract] [Full Text] [PDF]

				V. Lagree, A. Froger, S. Deschamps, J.-F. Hubert, C. Delamarche, G. Bonnec, D. Thomas, J. Gouranton, and I. Pellerin Switch from an Aquaporin to a Glycerol Channel by Two Amino Acids Substitution J. Biol. Chem., March 12, 1999; 274(11): 6817 - 6819. [Abstract] [Full Text] [PDF]

				V. Lagree, A. Froger, S. Deschamps, I. Pellerin, C. Delamarche, G. Bonnec, J. Gouranton, D. Thomas, and J.-F. Hubert Oligomerization State of Water Channels and Glycerol Facilitators. INVOLVEMENT OF LOOP E J. Biol. Chem., December 18, 1998; 273(51): 33949 - 33953. [Abstract] [Full Text] [PDF]

				M. Bonhivers, J. M. Carbrey, S. J. Gould, and P. Agre Aquaporins in Saccharomyces. GENETIC AND FUNCTIONAL DISTINCTIONS BETWEEN LABORATORY AND WILD-TYPE STRAINS J. Biol. Chem., October 16, 1998; 273(42): 27565 - 27572. [Abstract] [Full Text] [PDF]