Search results for "Signal peptide"
showing 10 items of 60 documents
Specific binding of VegT mRNA localization signal to membranes in Xenopus oocytes
2021
Abstract We have studied the interaction of a VegT mRNA localization signal sequence with the membranes of the mitochondrial cloud in Xenopus oocytes, and the binding of the VegT mRNA signal sequence to the lipid raft regions of the vesicles bounded by ordered and disordered phospholipid bilayers. RNA preference for the membranes of the mitochondrial cloud was confirmed using microscopy of a fluorescence resonance energy transfer from RNA molecules to membranes. Our studies show that VegT mRNA has a higher affinity for ordered regions of lipid bilayers. This conclusion is supported by the dissociation constant measurements for RNA-liposome complex and the visualization of the FRET signal be…
Characterization of a cDNA clone encoding a glycine-rich cuticular protein of Tenebrio molitor: developmental expression and effect of a juvenile hor…
1992
0962-1075 (Print) Journal Article; The complete sequence of a cDNA clone, isolated from epidermal mRNA of Tenebrio molitor using a monoclonal antibody raised against an adult-specific cuticular antigen only present in the hard cuticle, was obtained after primer extension at the 5' end. From this cDNA sequence, the deduced protein encompasses 199 amino acids (including a signal peptide) with a total molecular weight of 20.7 kDa. The protein exhibits a bipartite structure: glycine-rich region located in its NH2-terminal part and a carboxy-terminal domain sharing homologies with other cuticular proteins of Orthoptera, Diptera and Lepidoptera. In-situ hybridization analysis shows that the corre…
Identification ofCandida albicanswall mannoproteins covalently linked by disulphide and/or alkali-sensitive bridges
2014
This paper describes the results obtained by analysing the human pathogen Candida albicans cell wall subproteome by mass spectrometry, using extraction procedures aimed at releasing proteins bound by disulphide bridges (RAE-CWP) or alkali-labile ester linkages (ALS-CWP). Ten of the total proteins released from the wall by β-ME and/or NaOH contained a potential signal peptide, lacked a GPI cell wall hydrophobic C-terminal domain and were identified as true wall proteins by in silico analysis, whereas four additional proteins were identified as bound to the plasma membrane. The results surprisingly demonstrated that, in addition to the expected RAE-CWP and ALS-CWP proteins, 16 GPI proteins we…
Secretion of the rotavirus VP8* protein inLactococcus lactis
2001
Secretion of the VP8* subunit of the VP4 capsid protein of rotavirus by Lactococcus lactis has been achieved. For this purpose, a secretion vector has been constructed with the lactococcal signal sequence AL9 and the VP8*-encoding gene fragment. The amount of VP8* secreted by L. lactis in the culture supernatant was quantified and visualised by Western blot. Furthermore, it was shown to retain its hemagglutination capability, indicating that the conformation of the secreted peptide may be retaining its biological activity.
Growth-dependent release of carbohydrate metabolism-related and antioxidant enzymes from Staphylococcus aureus strain 6 as determined by proteomic an…
2011
Proteins released into the culture medium by Staphylococcus aureus (S. aureus) strain 6 were determined at the end of the exponential growth phase (4.5 h). Eleven proteins were identified by liquid chromatography coupled with mass spectrometry. Three proteins were predicted to have signal peptides indicating their extracellular localization. The other proteins were presumably located in the cytoplasm of the bacteria. Five out of the 11 proteins were involved in carbo- hydrate metabolism. Other intracellular proteins of S. aureus were not detected in the culture medium. This indicates that the release of these 11 proteins was specific and that unspecific protein release due to damaged or dyi…
Dissection of the structure-forming activity from the structure-guiding activity of silicatein: a biomimetic molecular approach to print optical fibe…
2020
Silicateins, a group of proteins forming the proteinaceous axial filaments of the inorganic biosilica spicules of the siliceous sponges, are unique in their dual function to exhibit both structure-guiding (providing the structural platform for the biosilica product) and structure-forming activities (enzymatic function: biosilica synthesis from ortho-silicate). The primary translation product of the silicatein gene comprises a signal peptide, a pro-peptide and, separated by an autocatalytic cleavage site glutamine/aspartic acid [Q/D], the sequence of the mature silicatein protein. In order to dissect the biocatalytic, structure-forming activity of silicatein from its structure-guiding functi…
Chloroplast signal length requirement reflects the outer membrane and TOC complex dimension
2015
Background and Purpose: The evolution of an efficient preprotein targeting and translocation system was a central prerequisite for the endosymbiotic integration of a -proteobacteria and cyanobacteria as cellular organelles. Today, it is widely accepted that during evolution most (pre-)proteins destined for these two organelles were equipped with an N-terminal targeting signal for localization. While multiple modes of evolution of these extensions are currently discussed, all evolved signals serve the same function – forming a signal for targeting to the correct organelle and translocation across both membranes. We aimed to generalize the current idea for the length requirement of the N-term…
Signal sequences modulate the immunogenic performance of human hepatitis C virus E2 gene
2005
Abstract Envelope protein E2 of human hepatitis C virus (HCV) is an attractive component of a prototype HCV vaccine. Delivered by DNA immunogens, E2 evokes specific immune response of Th1-type, failing to induce either considerable antibody production, or T-helper cell proliferation. We aimed at modulating the immunogenic performance of E2 gene by changing the mode of protein expression in eukaryotic cells. Plasmids were constructed encoding full-length E2 and nonstructural protein 1 (p7) fused to either 13 or 38 C-terminal amino acids (aa) of HCV E1 that contain second hydrophobic segment of E1 stop-transfer signal, or a complete E1 stop-transfer signal with duplicated second hydrophobic s…
Response to Comment on “Characterizing the N-Terminal Processing Motif of MHC Class I Ligands”
2008
The possibility that ERAAP plays a role in limiting the presentation of peptides derived from signal peptides may be tempting from an immunologist’s view. In eukaryotic cells, signal peptides have a mean length of 22 amino acids and are removed by signal peptide peptidases from the N terminus of
A point mutation in the Ncr1 signal peptide impairs the development of innate lymphoid cell subsets.
2018
International audience; NKp46 (CD335) is a surface receptor shared by both human and mouse natural killer (NK) cells and innate lymphoid cells (ILCs) that transduces activating signals necessary to eliminate virus-infected cells and tumors. Here, we describe a spontaneous point mutation of cysteine to arginine (C14R) in the signal peptide of the NKp46 protein in congenic Ly5.1 mice and the newly generated NCR(B6C14R) strain. Ly5.1(C14R) NK cells expressed similar levels of Ncr1 mRNA as C57BL/6, but showed impaired surface NKp46 and reduced ability to control melanoma tumors in vivo. Expression of the mutant NKp46(C14R) in 293T cells showed that NKp46 protein trafficking to the cell surface …