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

J. Biol. Chem., Vol. 283, Issue 52, 36386-36396, December 26, 2008

This Article Full Text Full Text (PDF) All Versions of this Article: 283/52/36386    most recent M803102200v1 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 Google Scholar Google Scholar Articles by Ramalingam, J. K. Articles by Preiser, P. R. Search for Related Content PubMed PubMed Citation Articles by Ramalingam, J. K. Articles by Preiser, P. R. Social Bookmarking                      What's this?

ATP/ADP Binding to a Novel Nucleotide Binding Domain of the Reticulocyte-binding Protein Py235 of Plasmodium yoelii^*

Jeya Kumar Ramalingam¹, Cornelia Hunke¹, Xiaohong Gao, Gerhard Grüber², and Peter Rainer Preiser³

From the Divisions of Genomics and Genetics and Structural and Computational Biology, School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551, Singapore

The mechanism by which a malaria merozoite recognizes a suitable host cell is mediated by a cascade of receptor-ligand interactions. In addition to the availability of the appropriate receptors, intracellular ATP plays an important role in determining whether erythrocytes are suitable for merozoite invasion. Recent work has shown that ATP secreted from erythrocytes signals a number of cellular processes. To determine whether ATP signaling might be involved in merozoite invasion, we investigated whether known plasmodium invasion proteins contain nucleotide binding motifs. Domain mapping identified a putative nucleotide binding region within all members of the reticulocyte-binding protein homologue (RBL) family analyzed. A representative domain, termed here nucleotide binding domain 94 (NBD94), was expressed and demonstrated to specifically bind to ATP. Nucleotide affinities of NBD94 were determined by fluorescence correlation spectroscopy, where an increase in the binding of ATP is observed compared with ADP analogues. ATP binding was reduced by the known F₁F₀-ATP synthase inhibitor 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole. Fluorescence quenching and circular dichroism spectroscopy of NBD94 after binding of different nucleotides provide evidence for structural changes in this protein. Our data suggest that different structural changes induced by ATP/ADP binding to RBL could play an important role during the invasion process.

Received for publication, April 23, 2008 , and in revised form, October 20, 2008.

^* This work was supported by Agency for Science, Technology and Research (A^*STAR) Biomedical Research Council Grant 06/1/22/19/456 and Academic Research Council Grant MLC03/03. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ Both authors made equal contributions to this work.

² To whom correspondence may be addressed. Tel.: 65-6316-2989; Fax: 65-6791-3856; E-mail: ggrueber{at}ntu.edu.sg. ³ To whom correspondence may be addressed. Tel.: 65-6316-2869; Fax: 65-6791-3856; E-mail: PRPreiser{at}ntu.edu.sg.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?