Bandell, M.

Geest, M. van

Lolkema, J.S.

Marty-Teysset, C.

English

Proceedings - University of Groningen

   University of GroningenThe 2-Hydroxy-Carboxylate Transporter FamilyLolkema, J.S.; Marty-Teysset, C.; Geest, M. van; Bandell, M.IMPORTANT NOTE: You are advised to consult the publisher's version (publisher's PDF) if you wish to cite fromit. Please check the document version below.Document VersionPublisher's PDF, also known as Version of recordPublication date:1996Link to publication in University of Groningen/UMCG research databaseCitation for published version (APA):Lolkema, J. S., Marty-Teysset, C., Geest, M. V., & Bandell, M. (1996). The 2-Hydroxy-CarboxylateTransporter Family.CopyrightOther than for strictly personal use, it is not permitted to download or to forward/distribute the text or part of it without the consent of theauthor(s) and/or copyright holder(s), unless the work is under an open content license (like Creative Commons).The publication may also be distributed here under the terms of Article 25fa of the Dutch Copyright Act, indicated by the “Taverne” license.More information can be found on the University of Groningen website: https://www.rug.nl/library/open-access/self-archiving-pure/taverne-amendment.Take-down policyIf you believe that this document breaches copyright please contact us providing details, and we will remove access to the work immediatelyand investigate your claim.Downloaded from the University of Groningen/UMCG research database (Pure): http://www.rug.nl/research/portal. For technical reasons thenumber of authors shown on this cover page is limited to 10 maximum.Download date: 04-06-2022C5 Membrane-bound carriers P-0-09 THE 2-HYDROXY-CARBOXYLATE TRANSPORTBR FAMILY LOLKEMA JS, MARTY-TBYSSET C, VAN GEEST M, BANDELL M. Department of Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen (NL) The homologous gene family consists of three known secondary transporters: the Na+-dependent citrate carrier of K. pneumoniae (CitS), the malate transporter of L. luctis (MleP) and the citrate caniers of lactic acid bacteria (CitP). Substrates of the transporters present the motif HO-C-COOH. Physiological substrates are citrate, malate and lactate. CitS functions as an uptake system for citrate under anaerobic conditions and is driven by the proton and sodium ion motive force. MleP and CitP are involved in secondary metabolic energy generation. Transport of the substrates results in the generation of a membrane potential. The family forms a distinct structural class of secondary transporters. Topological studies with CitS indicate that the protein is folded in 9 transmembrane segments with the N-terminal in the cytoplasm and the C-terminal in the periplasm. P-C5--11 SPECIFIC BINDING OF THE STILBENE DERIVATIVE TO THE MITCKXONDRlAL ADP/ATP CARRIER IvWIMA E,’ SHiNO~ Y,’ TERADA H.’ ‘APRO Life Sci. Inst., Naruto (IPN), Pac. Pharm. Sci., Univ. of Tokushima (JPN) Purpose: Determination of the effect of 4, 4’- diisothiocyano-2, 2’4lbene disulfonate @IDS) on the mitochondrial ADP/ATP carrier @AC). Methods: Bovine heart mitoohondria and their in- verted vesicles were treated with various concen- trationsof DIDSforlOminat25”C. ResuIfsz DIDS inhibited ADP uptake via AAC of inverbsd vesicles, but not mitochokiria. Of the mitochontial membrane proteins, D?DS was found to interact specifically on1 Treatment of the vesicles with DID g ?e. J#+c. mhlbded the specific labeling of Cysts9 by eosin-5-maleimide (EI+), although DIPS morhfied only LTV. In add&on, labelmg by DIDS was camp ete y mhib- ited by retkttnent of the vesicles with bo kit aci a %e- which is a rt inhibitor achng -37 *%om the matrix side, but not acted by treatment with carboxyatr@yloside, &ich is a transport inhibi- tor aatitsg &&I the cytosolic side, did not af%‘ct la- P-c5-10 MERC, A MEMBRANE PROTEIN INVOLVED IN TRANSPORT OF MERCURIC IONS. SAHLMAN, L.‘, POWLOWSKJ, J.* ‘Dept. of Biochem., Univ. of Ume& (Sweden) 2Dept. of Chem. and Biochem., Concordia Univ. (Canada) Purpose: Some mercuric ion resistant bacteria have one inner membrane mercuric ion resistance protein, while others have two. E.coli, which normally has MerT and MerC, seems to detoxify Hg*’ when MerC is absent. We therefore wanted to investigate the properties and function of MerC. Methods: MerC was cloned and overproduced in E.coli. The protein was purified using two chromatography steps. Transport was studied in whole cells and vesicles. Results: Cells expressing MerC were able to transport Hg*+: cysteine residues were shown to be functionally important. Transport was also observed in Me&containing vesicles. Triton X-l 00 solubilized MerC was purified to homogeneity. Conclusions: MerC appears to play a transport role in the detoxification of Hg”. P-CS-12 THERMOQYNA&XIC PROPERTIES IN CELL IklEMaRANES QINC-DONG ‘&HANG, LWGYUN Zl3ANC.t ‘H&i bapitd dmology rad ct+stat&s, Tiaq$n 30015O(CN)‘, Inst. of Pars., CAS, l&&&t 1 ‘W Purpose: We consider nonlinear solitary w&es (solitous) which may result from local membrane disorder in the preat~nce of an electric field across the cell membrane. The thermodynamic prop&k+ of ceil membrane such as critical temp&ature and specific heat is investigated. Methods: in this paper, the soliton statistics method is applied to explaiu the thermodynamic properties iu cell membrane. Our ‘theoretical analysis points out the possible existence of several kinds of’or’kntatiou waves iu a liquid-crystalline structure of a cell membrane. It is also proved that the structure of a cell membrane satisfies the SkOordou field form. The critical tempwature and the coefficient of linear specific heat of cell membrane are stud&d from the s&ton statistics. Results: The theoretical valuea of thermodynamic properties in cell membraue is obtained by statietica approach. We have compared with the experimental values. aud find the theoretical and erp&nental va1ues.k consistent. Conclusions: The agreement between theoretical and experimental values for ce.ll membrane t+ugeests that the soliton model gives a reasonable explunatiou of 041 membraue. 134 

The 2-Hydroxy-Carboxylate Transporter Family

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The 2-Hydroxy-Carboxylate Transporter Family

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