Blaauwen, T. den

Does, C. van der

Driessen, A.J.M.

English

ARTS repository - University of Groningen

   University of GroningenSecA Exposes a Carboxy-Terminal Domain to the PeriplasmDoes, C. van der; Blaauwen, T. den; Driessen, A.J.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):Does, C. V. D., Blaauwen, T. D., & Driessen, A. J. M. (1996). SecA Exposes a Carboxy-Terminal Domainto the Periplasm.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: 01-02-2024C5 Membrane-bound carriers P-c501 SECAEXPQ%SkWW-W DO&UN?0 THE PERPLASM. VAN DEB DoI33 C, DEN BLAAUWEN T, AND DRIESSEN, A J M. Dep. of Microbial. and the Groningen Biomol. Sci. and Eiotechn. Institute, Univ. of Groningen, NL. Purpose : To elucidate the structure/function of the bacterial prepmtein @an&case consisting of the membrane bound components SecY, SecE and Se& and the peripheral ATPase SecA. Methods ami Results : SecY, SecE and Se& Wete overcxpre.ssed from a synthetic operon. SecYEG’ v~ic1e.s showed an increase in translocation and preprot& stimulated translocation ATPase activity, demonstrating the functionat overexpression. Fu&e.rmore, overexpression of SecYEG leads to increased SecA membrane bind&, mainly at the expense of the cytosolic SecA pool. The membrane associated conformation of SecA was analysed by trypsin digestion, immune precipitation, and mdeimide labeling of SecA in right-side out and inside out membrane vesicles. These expat’iments show that SecA, under non translocating conditions expme.9 a 5 kD domain to the PeriplapmiC side. zhis 5 kD domain was identified as the carboxy-terminus. Conclusions : SecA is an intrinsic subunit of the E. cofi preprotein transiocaJe and protrudes, even under non trunslocating conditions, the membrane with its afboxy-terminal tail. P-C%03 EFFECT OF POLYPRENYL DIPHOSPHATE ON PERMEABILITY AND STABILITY OF MEMtlRANES IJANAS T., 2JANAS T., lWALI@KA K. IDept. Biophysics, Pedagogical Univ., Zi&nr G&a (PL) *ht. Physics, Technical Univ., Zielona G&a (PL) Purpose: Phosphopolyisoprenols function as a hydrophobic carrier of glycosyl units across membranes during glycosylation teactions in cells. The influence of hexadecaprenyl diphos- phate (C80-PP) on permeability and stability of bilayer lipid membranes made from dioleoyl- phosphatidylcholine or its mixNre with C80-PP was studied. Methods: Current-voltage characteristics, con- ductance-temperature nlationships, membrane capacitance and membrane breakdown voltage have been studied. Membrane hydrophobic thick- ness and the activation energy for ion migration have been determined. Redts: CSO-PP incnases the activation energy for ion migration and the membrane electro- mechanical Stability, and slightly changes the membrane hydrophobic thickness. Conclusions: We conclude that C80-PP can modulate the permeability and stability of model lipid membranes. (supported by grant SCSR no. 6 PO4A 014 10) P-cZ5-02 SOLUBIL~ZJ~TIOM AND PJJB& ,,ICATIQN OF THB AbPfATP-C&#Rt R FROM lllFCHICKEN HEART MITOC!~W~ DOLDER M,l TON J,2 STACFI‘OWIAK 0,l WALLIMANN T.1 11nst. of cell Biology, ETH. Zuerich (CFI)). *CBLE, Univ. of Utrecht, (NL). Purpose: Current protocols for the mitochondrial carriers including tg u&cation of e ADPJATP- carrier (AAC) involve chromat@ra h (IPJ of Ttiton X-100 extracts on hyriroxyapatite A . We have analyzed the efficiency of other non-ionic deter- gents for AAC solubilization. In addition, binding of protein-detergent mieelles to different ion-ex- than e resins was analyzed. The goal is to purify AA&n detergents suitable for protein crystalliza- tion. Methods: Mitochondria were solubilized with a variety of deter enb protein qd A &; and the extracts anaIyzed for C content. SolubiIized proteins were applied to different ian-exchange columns. Binding and elution of AAC was momtored. Results: The most Conclusions: The binding and elution characteri- stics of AAC to HA are stron the detergent. In contrast, we a& ly determined by anion- or cation. exchangers provide a tool for carrier purification which is largely independent of the detergent. P-CS-04 TRANSPORT OF IONS ACROSS MODEL MEMBRANES MODIIWD BY POLYPRENYL MUNOF##3BiWATE 1JANAS T.. 2JANAS T. lhst. physics, Technical Univ.. Zielona Bra (PL). *Dept. Biophysics, Pedagogical Univ., Ziclona G&a (PL) Purpose: Polyprenyl phosphates are involved in glycosylation reactions as a transmembrane carrier lipid. The influence of polyplenyl mono- phosphate on ion permeability of bilayer lipid membranes made from dioleoylphospbatidyl- choline or its mixture with polyprenyl mono- phosphate was studied. Methods: Steady-state diffusion potentials, current-voltage characteristics and conductance- temperature relationships have been studied. Membrane permeability coefficients for sodium and chloride ions and the activation energy for ion migration have been determined. Results: Polyprenyl monophosphate: -decreases membrane permeability coefficients both for sodium and chloride ions: -increases the transfe- rence number for sodium ions and the activation energy for ion migration across lipid biiyer. Conclusions: The results indicate that poly- prenyl monophosphate molecules can modulate the transport properties of membranes. (supported by grant SCSR no. 6 PO4A 014 10) 132 

SecA Exposes a Carboxy-Terminal Domain to the Periplasm

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SecA Exposes a Carboxy-Terminal Domain to the Periplasm

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