Functional characterization of the LCMV GP-C signal peptide [Elektronische Ressource] / Sabrina Schrempf

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Functional Characterizationof the LCMV GP-C Signal PeptideSabrina Schrempf2008INAUGURAL - DISSERTATIONsubmitted to theCombined Faculties for the Natural Sciences and for Mathematicsof the Ruperto-Carola University of Heidelbergfor the degree ofDoctor of Natural Sciencespresented byDiplom-Biochemikerin Sabrina Schrempffrom GelnhausenDate of oral examination: :::::::::::::::Functional Characterizationof the LCMV GP-C Signal PeptideReferees:Prof. Dr. Bernhard DobbersteinProf. Dr. Irmgard SinningFur Oliver,der mich immer au angtundfur meine Eltern,die mich stets unterstutzen.AbstractN-terminal signal sequences of secretory and membrane proteins mediate targeting toand translocation across the endoplasmic reticulum (ER) membrane. After membraneinsertion, signal sequences are in most cases cleaved from the precursor protein by signalpeptidase (SPase). Signal sequences are usually 15 to 25 amino acid residues in lengthand have a typical tripartite structure with a central hydrophobic core of about 7 to 10residues, a polar N-terminal region, and a short C-terminal region which contains theSPase cleavage site.Insertion of the lymphocytic choriomeningitis virus (LCMV) precursor glycoprotein C(pGP-C) into the membrane of the ER is mediated by an unusual signal sequence. Itcomprises 58 amino acid residues and contains an extended N-terminal region including amyristoylation consensus site and two hydrophobic regions separated by a lysine residue.



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Published 01 January 2008
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