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Long-lived Signal Peptide of Lymphocytic Choriomeningitis Virus Glycoprotein pGP-C

Long-lived Signal Peptide of Lymphocytic Choriomeningitis Virus Glycoprotein pGP-C


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FROESCHKE, Marc, Michael BASLER, Marcus GRÖTTRUP, Bernhard DOBBERSTEIN, 2003. Long-lived Signal Peptide of Lymphocytic Choriomeningitis Virus Glycoprotein pGP-C. In: Journal of Biological Chemistry. 278(43), pp. 41914-41920. ISSN 0021-9258. eISSN 1083-351X

@article{Froeschke2003-10-24Long--22135, title={Long-lived Signal Peptide of Lymphocytic Choriomeningitis Virus Glycoprotein pGP-C}, year={2003}, doi={10.1074/jbc.M302343200}, number={43}, volume={278}, issn={0021-9258}, journal={Journal of Biological Chemistry}, pages={41914--41920}, author={Froeschke, Marc and Basler, Michael and Gröttrup, Marcus and Dobberstein, Bernhard} }

<rdf:RDF xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bibo="http://purl.org/ontology/bibo/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:dcterms="http://purl.org/dc/terms/" xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > <rdf:Description rdf:about="https://kops.uni-konstanz.de/rdf/resource/123456789/22135"> <dcterms:bibliographicCitation>The journal of biological chemistry : JBC ; 278 (2003), 43. - S. 41914-41920</dcterms:bibliographicCitation> <dc:language>eng</dc:language> <dcterms:title>Long-lived Signal Peptide of Lymphocytic Choriomeningitis Virus Glycoprotein pGP-C</dcterms:title> <dc:creator>Gröttrup, Marcus</dc:creator> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2013-03-12T10:12:06Z</dcterms:available> <dcterms:issued>2003-10-24</dcterms:issued> <dc:contributor>Dobberstein, Bernhard</dc:contributor> <dc:creator>Dobberstein, Bernhard</dc:creator> <dcterms:abstract xml:lang="eng">Signal peptides (SPs) direct nascent secretory and membrane proteins to the membrane of the endoplasmic reticulum. They are usually cleaved from the nascent polypeptide by signal peptidase and then further proteolytically processed. The SP of the pre-glycoprotein (pGP-C) of the lymphocytic choriomeningitis virus SPGP-C (signal peptide of pGP-C) shows different properties: 1) The SPGP-C is unusually long (58 amino acid residues) and contains two hydrophobic segments interrupted by a lysine residue. 2) The SPGP-C is cleaved only from a subset of pGP-C proteins. A substantial portion of pGP-C accumulates that still contains the SPGP-C.3)The cleaved SPGP-C is rather long-lived (t(1/2) of more than 6 h). 4) The cleaved SPGP-C resides in the membrane and is resistant to digestion with proteinase K even in the presence of detergents, suggesting a very compact structure. 5) SPGP-C accumulates in virus particles. These unusual features of the cleaved SPGP-C suggest that SPGP-C not only targets the nascent pGP-C to the endoplasmic reticulum membrane but also has additional functions in lymphocytic choriomeningitis virus life cycle.</dcterms:abstract> <dc:contributor>Basler, Michael</dc:contributor> <dc:contributor>Gröttrup, Marcus</dc:contributor> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/22135"/> <dc:contributor>Froeschke, Marc</dc:contributor> <dc:creator>Froeschke, Marc</dc:creator> <dcterms:rights rdf:resource="http://nbn-resolving.org/urn:nbn:de:bsz:352-20140905103605204-4002607-1"/> <dc:creator>Basler, Michael</dc:creator> <dc:rights>deposit-license</dc:rights> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2013-03-12T10:12:06Z</dc:date> </rdf:Description> </rdf:RDF>

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