Expression of the pCloDF13 encoded bacteriocin release protein or its stable signal peptide causes early effects on protein biosynthesis and Mg2+ transport

1995 ◽  
Vol 67 (3) ◽  
pp. 255-260 ◽  
Author(s):  
Freek Stegehuis ◽  
Fimme J. van der Wal ◽  
Joen Luirink ◽  
Bauke Oudega
Keyword(s):  
Signal Peptide ◽  
Protein Biosynthesis ◽  
Early Effects ◽  
Bacteriocin Release Protein ◽  
Stable Signal

Functioning of the stable signal peptide of the pCloDF13-encoded bacteriocin release protein

1991 ◽  
Vol 5 (2) ◽  
pp. 393-399 ◽  
Author(s):  
J. Luirink ◽  
B. Duim ◽  
J. W. L. Gier ◽  
B. Oudega
Keyword(s):  
Signal Peptide ◽  
Bacteriocin Release Protein ◽  
Stable Signal

scholarly journals Role of the Stable Signal Peptide and Cytoplasmic Domain of G2 in Regulating Intracellular Transport of the Junín Virus Envelope Glycoprotein Complex

2006 ◽  
Vol 80 (11) ◽  
pp. 5189-5198 ◽  
Author(s):  
Sudhakar S. Agnihothram ◽  
Joanne York ◽  
Jack H. Nunberg
Keyword(s):  
Cell Surface ◽  
Signal Peptide ◽  
Envelope Glycoprotein ◽  
Intracellular Transport ◽  
Cytoplasmic Domain ◽  
Virus Envelope ◽  
Quality Control Process ◽  
C Complex ◽  
Stable Signal

ABSTRACT Enveloped viruses utilize the membranous compartments of the host cell for the assembly and budding of new virion particles. In this report, we have investigated the biogenesis and trafficking of the envelope glycoprotein (GP-C) of the Junín arenavirus. The mature GP-C complex is unusual in that it retains a stable signal peptide (SSP) as an essential component in association with the typical receptor-binding (G1) and transmembrane fusion (G2) subunits. We demonstrate that, in the absence of SSP, the G1-G2 precursor is restricted to the endoplasmic reticulum (ER). This constraint is relieved by coexpression of SSP in trans, allowing transit of the assembled GP-C complex through the Golgi and to the cell surface, the site of arenavirus budding. Transport of a chimeric CD4 glycoprotein bearing the transmembrane and cytoplasmic domains of G2 is similarly regulated by SSP association. Truncations to the cytoplasmic domain of G2 abrogate SSP association yet now permit transport of the G1-G2 precursor to the cell surface. Thus, the cytoplasmic domain of G2 is an important determinant for both ER localization and its control through SSP binding. Alanine mutations to either of two dibasic amino acid motifs in the G2 cytoplasmic domain can also mobilize the G1-G2 precursor for transit through the Golgi. Taken together, our results suggest that SSP binding masks endogenous ER localization signals in the cytoplasmic domain of G2 to ensure that only the fully assembled, tripartite GP-C complex is transported for virion assembly. This quality control process points to an important role of SSP in the structure and function of the arenavirus envelope glycoprotein.

scholarly journals Human endogenous retrovirus HERV-K(HML-2) encodes a stable signal peptide with biological properties distinct from Rec

Retrovirology ◽  
2009 ◽  
Vol 6 (1) ◽  
pp. 17 ◽  
Author(s):  
Alessia Ruggieri ◽  
Esther Maldener ◽  
Marlies Sauter ◽  
Nikolaus Mueller-Lantzsch ◽  
Eckart Meese ◽  
...  
Keyword(s):  
Signal Peptide ◽  
Biological Properties ◽  
Endogenous Retrovirus ◽  
Human Endogenous Retrovirus ◽  
Stable Signal

scholarly journals The role of proteolytic processing and the stable signal peptide in expression of the Old World arenavirus envelope glycoprotein ectodomain

Virology ◽  
2013 ◽  
Vol 436 (1) ◽  
pp. 127-133 ◽  
Author(s):  
Dominique J. Burri ◽  
Antonella Pasquato ◽  
Joel Ramos da Palma ◽  
Sebastien Igonet ◽  
Michael B.A. Oldstone ◽  
...  
Keyword(s):  
Signal Peptide ◽  
Envelope Glycoprotein ◽  
Proteolytic Processing ◽  
Old World ◽  
Stable Signal

scholarly journals Intramolecular quality control: HIV-1 Envelope gp160 signal-peptide cleavage as a functional folding checkpoint

2020 ◽  
Author(s):  
Nicholas McCaul ◽  
Matthias Quandte ◽  
Ilja Bontjer ◽  
Guus van Zadelhoff ◽  
Aafke Land ◽  
...  
Keyword(s):  
Quality Control ◽  
Signal Peptide ◽  
Protein Biosynthesis ◽  
Protein Structures ◽  
Secretory Protein ◽  
Viral Fitness ◽  
Secretory Proteins ◽  
Redox Active ◽  
Hiv 1 ◽  
Redox Active Cysteine

SummaryRemoval of the membrane-tethering signal peptides that target secretory proteins to the endoplasmic reticulum is a prerequisite for proper folding. While generally thought to be removed well before translation termination, we here report two novel post-targeting functions for the HIV-1 gp120 signal peptide, which remains attached until gp120 folding triggers its removal. First, the signal peptide improves fidelity of folding by enhancing conformational plasticity of gp120 by driving disulfide isomerization through a redox-active cysteine, at the same time delaying folding by tethering the N-terminus to the membrane, which needs assembly with the C-terminus. Second, its carefully timed cleavage represents intramolecular quality control and ensures release and stabilization of (only) natively folded gp120. Postponed cleavage and the redox-active cysteine both are highly conserved and important for viral fitness. Considering the ∼15% secretory proteins in our genome and the frequency of N-to-C contacts in protein structures, these regulatory roles of the signal peptide are bound to be more common in secretory-protein biosynthesis.

scholarly journals Bitopic Membrane Topology of the Stable Signal Peptide in the Tripartite Junín Virus GP-C Envelope Glycoprotein Complex

2007 ◽  
Vol 81 (8) ◽  
pp. 4331-4337 ◽  
Author(s):  
Sudhakar S. Agnihothram ◽  
Joanne York ◽  
Meg Trahey ◽  
Jack H. Nunberg
Keyword(s):  
Membrane Fusion ◽  
Signal Peptide ◽  
Envelope Glycoprotein ◽  
Lipid Membrane ◽  
Critical Role ◽  
Membrane Topology ◽  
Single Amino Acid ◽  
Fusion Activity ◽  
C Complex ◽  
Stable Signal

ABSTRACT The stable signal peptide (SSP) of the GP-C envelope glycoprotein of the Junín arenavirus plays a critical role in trafficking of the GP-C complex to the cell surface and in its membrane fusion activity. SSP therefore may function on both sides of the lipid membrane. In this study, we have investigated the membrane topology of SSP by confocal microscopy of cells treated with the detergent digitonin to selectively permeabilize the plasma membrane. By using an affinity tag to mark the termini of SSP in the properly assembled GP-C complex, we find that both the N and C termini reside in the cytosol. Thus, SSP adopts a bitopic topology in which the C terminus is translocated from the lumen of the endoplasmic reticulum to the cytoplasm. This model is supported by (i) the presence of two conserved hydrophobic regions in SSP (hφ1 and hφ2) and (ii) our previous demonstration that lysine-33 in the ectodomain loop is essential for pH-dependent membrane fusion. Moreover, we demonstrate that the introduction of a charged side chain or single amino acid deletion in the membrane-spanning hφ2 region significantly diminishes SSP association in the GP-C complex and abolishes membrane fusion activity. Taken together, our results suggest that bitopic membrane insertion of SSP is centrally important in the assembly and function of the tripartite GP-C complex.

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