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

Froeschke, Marc; Basler, Michael; Gröttrup, Marcus; Dobberstein, Bernhard

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

Dateien

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Datum

2003

Autor:innen

Froeschke, Marc

Basler, Michael

Gröttrup, Marcus

Dobberstein, Bernhard

Open Access-Veröffentlichung

Open Access Green

Sammlungen

Biologie

Publikationstyp

Zeitschriftenartikel

Publikationsstatus

Published

Erschienen in

Journal of Biological Chemistry. 2003, 278(43), pp. 41914-41920. ISSN 0021-9258. eISSN 1083-351X. Available under: doi: 10.1074/jbc.M302343200

Zusammenfassung

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.

Fachgebiet (DDC)

570 Biowissenschaften, Biologie

Zitieren

ISO 690

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. 2003, 278(43), pp. 41914-41920. ISSN 0021-9258. eISSN 1083-351X. Available under: doi: 10.1074/jbc.M302343200

BibTex

@article{Froeschke2003-10-24Longl-22135,
  year={2003},
  doi={10.1074/jbc.M302343200},
  title={Long-lived Signal Peptide of Lymphocytic Choriomeningitis Virus Glycoprotein pGP-C},
  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}
}

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    <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>
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