scholarly journals C-terminal Recognition by 14-3-3 Proteins for Surface Expression of Membrane Receptors

2005 ◽  
Vol 280 (43) ◽  
pp. 36263-36272 ◽  
Author(s):  
Brian Coblitz ◽  
Sojin Shikano ◽  
Meng Wu ◽  
Sandra B. Gabelli ◽  
Lisa M. Cockrell ◽  
...  
Keyword(s):  
Genetic Selection ◽  
Surface Expression ◽  
Membrane Receptors ◽  
Binding Modes ◽  
Mode Iii ◽  
Binding Motifs ◽  
Random Peptide Library ◽  
Random Peptide ◽  
Native Proteins ◽  
Localization Signal

Diverse functions of 14-3-3 proteins are directly coupled to their ability to interact with targeted peptide substrates. RSX(pS/pT)XP and RXΦX(pS/pT)XP are two canonical consensus binding motifs for 14-3-3 proteins representing the two common binding modes, modes I and II, between 14-3-3 and internal peptides. Using a genetic selection, we have screened a random peptide library and identified a group of C-terminal motifs, termed SWTY, capable of overriding an endoplasmic reticulum localization signal and redirecting membrane proteins to cell surface. Here we report that the C-terminal SWTY motif, although different from mode I and II consensus, binds tightly to 14-3-3 proteins with a dissociation constant (KD) of 0.17 μm, comparable with that of internal canonical binding peptides. We show that all residues but proline in -SWTX-COOH are compatible for the interaction and surface expression. Because SWTY-like sequences have been found in native proteins, these results support a broad significance of 14-3-3 interaction with protein C termini. The C-terminal binding consensus, mode III, represents an expansion of the repertoire of 14-3-3-targeted sequences.

scholarly journals Sequestration of Zinc Oxide by Fimbrial Designer Chelators

2000 ◽  
Vol 66 (1) ◽  
pp. 10-14 ◽  
Author(s):  
Kristian Kjærgaard ◽  
Jack K. Sørensen ◽  
Mark A. Schembri ◽  
Per Klemm
Keyword(s):  
Peptide Library ◽  
Zinc Binding ◽  
Polluted Water ◽  
Specific Sequence ◽  
Binding Motifs ◽  
Random Peptide Library ◽  
Random Peptide ◽  
Metal Chelating ◽  
Significant Homology

ABSTRACT Type 1 fimbriae are surface organelles of Escherichia coli. By engineering a structural component of the fimbriae, FimH, to display a random peptide library, we were able to isolate metal-chelating bacteria. A library consisting of 4 × 107 independent clones was screened for binding to ZnO. Sequences responsible for ZnO adherence were identified, and distinct binding motifs were characterized. The sequences selected exhibited various degrees of affinity and specificity towards ZnO. Competitive binding experiments revealed that the sequences recognized only the oxide form of Zn. Interestingly, one of the inserts exhibited significant homology to a specific sequence in a putative zinc-containing helicase, which suggests that searches such as this one may aid in identifying binding motifs in nature. The zinc-binding bacteria might have a use in detoxification of metal-polluted water.

36. Random Peptide Library Based on a Spider Neurotoxin, and Utilization of the Library in in vitro Evolution Directed to GPCR Ligands

Toxicon ◽  
2012 ◽  
Vol 60 (2) ◽  
pp. 113 ◽  
Author(s):  
Tai Kubo ◽  
Seigo Ono ◽  
Tadashi Kimura ◽  
Suzuko Kobayashi ◽  
Tetsuro Kondo ◽  
...  
Keyword(s):  
Peptide Library ◽  
In Vitro Evolution ◽  
Random Peptide Library ◽  
Random Peptide

Definition of the peptide mimotope of cellular receptor for hepatitis C virus E2 protein using random peptide library

2001 ◽  
Vol 1 (1) ◽  
pp. 77
Author(s):  
In-Hee Lee ◽  
Jae-Eun Paik ◽  
Sang-Yong Seol ◽  
Dae-Hyun Seog ◽  
Sae-Gwang Park ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Peptide Library ◽  
Cellular Receptor ◽  
E2 Protein ◽  
Random Peptide Library ◽  
Random Peptide ◽  
Definition Of

Isolation of lung tumor specific peptides from a random peptide library: generation of diagnostic and cell-targeting reagents

2003 ◽  
Vol 202 (2) ◽  
pp. 219-230 ◽  
Author(s):  
Tsuksa Oyama ◽  
Kathryn F. Sykes ◽  
Kausar N. Samli ◽  
John D. Minna ◽  
Stephen Albert Johnston ◽  
...  
Keyword(s):  
Lung Tumor ◽  
Peptide Library ◽  
Cell Targeting ◽  
Random Peptide Library ◽  
Random Peptide

scholarly journals Cell surface expression of murine, rat, and human Fc receptors by Xenopus oocytes.

1984 ◽  
Vol 160 (2) ◽  
pp. 606-611 ◽  
Author(s):  
E Pure ◽  
A D Luster ◽  
J C Unkeless
Keyword(s):  
Plasma Membrane ◽  
Cell Line ◽  
Surface Expression ◽  
Gamma Interferon ◽  
Membrane Receptors ◽  
Cell Surface Expression ◽  
Xenopus Laevis Oocytes ◽  
High Avidity ◽  
U937 Cells ◽  
Mouse Igg2a

We report that Xenopus laevis oocytes can efficiently translate and insert heterologous membrane receptors into the oocyte plasma membrane, where they can be detected by the binding of either monoclonal antibodies or ligands. Thus, oocytes injected with mRNA from the mouse J774 macrophage-like cell line, the rat RBL-1 basophilic leukemia, and the U937 promonocyte cell line, bound 2.4G2 Fab, rat IgE, and mouse IgG2a, respectively. The increase in the high avidity Fc gamma R observed after gamma-interferon induction of U937 cells was also observed after injection of mRNA from gamma-interferon-induced U937 cells into oocytes. This suggests either much greater message stability or a greater rate of transcription of Fc gamma Rhi mRNA in the gamma-interferon-induced cells. The assay affords a sensitive method for the detection of rare mRNA species that code for plasma membrane proteins.

scholarly journals Identification of Peptides That Inhibit the DNA Binding, trans-Activator, and DNA Replication Functions of the Human Papillomavirus Type 11 E2 Protein

2004 ◽  
Vol 78 (5) ◽  
pp. 2637-2641 ◽  
Author(s):  
Su-Jun Deng ◽  
Kenneth H. Pearce ◽  
Eric P. Dixon ◽  
Kelly A. Hartley ◽  
Thomas B. Stanley ◽  
...  
Keyword(s):  
Cell Culture ◽  
Human Papillomavirus ◽  
Dna Replication ◽  
Transcriptional Activation ◽  
Synthetic Peptides ◽  
Dna Interaction ◽  
Peptide Library ◽  
Random Peptide Library ◽  
Random Peptide

ABSTRACT Peptide antagonists of the human papillomavirus type 11 (HPV-11) E2-DNA association were identified using a filamentous bacteriophage random peptide library. Synthetic peptides antagonized the E2-DNA interaction, effectively blocked E2-mediated transcriptional activation of a reporter gene in cell culture, and inhibited E1-E2-mediated HPV-11 DNA replication in vitro. These peptides may prove to be useful tools for characterizing E2 function and for exploring the effectiveness of E2-inhibitor-based treatments for HPV-associated diseases.

Mimotope of Leptospira from phage-displayed random peptide library is reactive with both monoclonal antibodies and patients’ sera

2006 ◽  
Vol 115 (1-3) ◽  
pp. 54-63 ◽  
Author(s):  
R TUNGTRAKANPOUNG ◽  
P PITAKSAJJAKUL ◽  
N NANGARM ◽  
W CHAICUMPA ◽  
P EKPO ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Peptide Library ◽  
Random Peptide Library ◽  
Random Peptide
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