untitled
<OAI-PMH schemaLocation=http://www.openarchives.org/OAI/2.0/ http://www.openarchives.org/OAI/2.0/OAI-PMH.xsd>
<responseDate>2018-01-15T15:40:46Z</responseDate>
<request identifier=oai:HAL:hal-00417492v1 verb=GetRecord metadataPrefix=oai_dc>http://api.archives-ouvertes.fr/oai/hal/</request>
<GetRecord>
<record>
<header>
<identifier>oai:HAL:hal-00417492v1</identifier>
<datestamp>2018-01-11</datestamp>
<setSpec>type:ART</setSpec>
<setSpec>subject:sdv</setSpec>
<setSpec>collection:CNRS</setSpec>
<setSpec>collection:UNIV-PARIS7</setSpec>
<setSpec>collection:IMPMC</setSpec>
<setSpec>collection:ALLINSP</setSpec>
<setSpec>collection:UPMC</setSpec>
<setSpec>collection:UNIV-REUNION</setSpec>
<setSpec>collection:USPC</setSpec>
<setSpec>collection:UNIV-AG</setSpec>
<setSpec>collection:UPMC_POLE_2</setSpec>
</header>
<metadata><dc>
<publisher>HAL CCSD</publisher>
<title lang=en>Functional analysis of human RhCG: comparison with E. coli ammonium transporter reveals similarities in the pore and differences in the vestibule</title>
<creator>Zidi-Yahiaoui, Nedjma</creator>
<creator>Callebaut, Isabelle</creator>
<creator>Genetet, Sandrine</creator>
<creator>Le Van Kim, Caroline</creator>
<creator>Cartron, Jean-Pierre</creator>
<creator>Colin, Yves</creator>
<creator>Ripoche, Pierre</creator>
<creator>Mouro-Chanteloup, Isabelle</creator>
<contributor>Protéines de la membrane érythrocytaire et homologues non-érythroides ; Université des Antilles et de la Guyane (UAG) - Institut National de la Transfusion Sanguine [Paris] (INTS) - Université Paris Diderot - Paris 7 (UPD7) - Université de la Réunion (UR) - Institut National de la Santé et de la Recherche Médicale (INSERM)</contributor>
<contributor>Institut de minéralogie et de physique des milieux condensés (IMPMC) ; Université Pierre et Marie Curie - Paris 6 (UPMC) - IPG PARIS - Université Paris Diderot - Paris 7 (UPD7) - Centre National de la Recherche Scientifique (CNRS)</contributor>
<description>International audience</description>
<source>ISSN: 0363-6143</source>
<source>EISSN: 1522-1563</source>
<source>American Journal of Physiology - Cell Physiology</source>
<publisher>American Physiological Society</publisher>
<identifier>hal-00417492</identifier>
<identifier>https://hal.archives-ouvertes.fr/hal-00417492</identifier>
<source>https://hal.archives-ouvertes.fr/hal-00417492</source>
<source>American Journal of Physiology - Cell Physiology, American Physiological Society, 2009, 297, pp.C537-C547. 〈10.1152/ajpcell.00137.2009.〉</source>
<identifier>DOI : 10.1152/ajpcell.00137.2009.</identifier>
<relation>info:eu-repo/semantics/altIdentifier/doi/10.1152/ajpcell.00137.2009.</relation>
<language>en</language>
<subject lang=en>ammonium transport</subject>
<subject lang=en>HEK cells</subject>
<subject lang=en>Rhesus family</subject>
<subject lang=en>pH variations</subject>
<subject lang=en>ammonia channel</subject>
<subject>[SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology</subject>
<type>info:eu-repo/semantics/article</type>
<type>Journal articles</type>
<description lang=en>Zidi-Yahiaoui N, Callebaut I, Genetet S, Le Van Kim C, Cartron JP, Colin Y, Ripoche P, Mouro-Chanteloup I. Functional analysis of human RhCG: comparison with E. coli ammonium transporter reveals similarities in the pore and differences in the vestibule. Am J Physiol Cell Physiol 297: C537–C547, 2009. First published June 24, 2009; doi:10.1152/ajpcell.00137.2009.—Rh glycoproteins are members of the ammonium transporter (Amt)/methylamine permease (Mep)/Rh family facilitating movement of NH3 across plasma membranes. Homology models constructed on the basis of the experimental structures of Escherichia coli AmtB and Nitrosomonas europaea Rh50 indicated a channel structure for human RhA (RhAG), RhB (RhBG), and RhC (RhCG) glycoproteins in which external and internal vestibules are linked by a pore containing two strictly conserved histidines. The pore entry is constricted by two highly conserved phenylalanines, “twin-Phe.” In this study, RhCG function was investigated by stopped-flow spectrofluorometry measuring kinetic pH variations in HEK293E cells in the presence of an ammonium gradient. The apparent unitary NH3 permeability of RhCG was determined and was found to be close to that of AmtB. With a site-directed mutagenesis approach, critical residues involved in Rh NH3 channel activity were highlighted. In the external vestibule, the importance of both the charge and the conformation of the conserved aspartic acid was shown. In contrast to AmtB, individual mutations of each phenylalanine of the twin-Phe impaired the function while the removal of both resulted in recovery of the transport activity. The impact of the mutations suggests that, although having a common function and a similar channel structure, bacterial AmtB and human Rh vary in several aspects of the NH3 transport mechanisms.</description>
<date>2009</date>
</dc>
</metadata>
</record>
</GetRecord>
</OAI-PMH>
