Synthetic Signal Peptides of Parathyroid Hormone: Probes for Components of the Secretory Apparatus

1989 ◽  
pp. 19-27
Author(s):  
Michael P. Caulfield ◽  
Le T. Duong ◽  
Michael Rosenblatt
Keyword(s):  
Parathyroid Hormone ◽  
Signal Peptides ◽  
Synthetic Signal ◽  
Secretory Apparatus

Perturbation of the lipid bilayer of model membranes by synthetic signal peptides

1987 ◽  
Vol 903 (3) ◽  
pp. 465-472 ◽  
Author(s):  
Ramakrishnan Nagaraj ◽  
Mercy Joseph ◽  
Gundlapally Laxma Reddy
Keyword(s):  
Lipid Bilayer ◽  
Model Membranes ◽  
Signal Peptides ◽  
Synthetic Signal

scholarly journals A Method for Computationally Constructing Eukaryotic Synthetic Signal Peptide Sequences

2021 ◽  
Author(s):  
Grant T Daly ◽  
Aishwarya Prakash ◽  
Ryan G. Benton ◽  
Tom Johnsten
Keyword(s):  
Amino Acids ◽  
Signal Peptide ◽  
Protein Sequences ◽  
Building Blocks ◽  
Computational Method ◽  
Signal Peptides ◽  
Sequence Prediction ◽  
Synthetic Signal ◽  
Eukaryotic Organisms ◽  
Ordered Pairs

We developed a computational method for constructing synthetic signal peptides from a base set of signal peptides (SPs) and non-SP sequences. A large number of structured "building blocks", represented as m-step ordered pairs of amino acids, are extracted from the base. Using a straightforward procedure, the building blocks enable the construction of a diverse set of synthetic SPs that could be utilized for industrial and therapeutic purposes. We have validated the proposed methodology using existing sequence prediction platforms such as Signal-BLAST and MULocDeep. In one experiment, 9,555 protein sequences were generated from a large randomly selected set of "building blocks". Signal-BLAST identified 8,444 (88%) of the sequences as signal peptides. In addition, the Signal-BLAST tool predicted that the generated synthetic sequences belonged to 854 distinct eukaryotic organisms. Here, we provide detailed descriptions and results from various experiments illustrating the potential usefulness of the methodology in generating signal peptide protein sequences.

scholarly journals Interactions of signal peptides with signal-recognition particle

1990 ◽  
Vol 266 (1) ◽  
pp. 149-156 ◽  
Author(s):  
A Robinson ◽  
O M R Westwood ◽  
B M Austen
Keyword(s):  
Signal Peptide ◽  
Wheat Germ ◽  
Signal Recognition Particle ◽  
Translation System ◽  
Secretory Proteins ◽  
Signal Peptides ◽  
Signal Recognition ◽  
Synthetic Signal ◽  
Cross Links

The mechanisms whereby isolated or synthetic signal peptides inhibit processing of newly synthesized prolactin in microsome-supplemented lysates from reticulocytes and wheat-germ were investigated. At a concentration of 5 microM, a consensus signal peptide reverses the elongation arrest imposed by the signal-recognition particle (SRP), and at higher concentrations in addition inhibits elongation of both secretory and non-secretory proteins. A photoreactive form of a synthetic signal peptide cross-links under u.v. illumination to the 54 kDa and 68 kDa subunits of SRP, whereas the major cross-linked protein produced after photoreaction of rough microsomes is of 45 kDa. As SRP-mediated elongation arrest is unlikely to be essential for translocation, it is suggested that signal peptides may interact with components other than SRP in the translation system in vitro.

The synthetic precursor specific region of pre-pro-parathyroid hormone forms ion channels in lipid bilayers

1988 ◽  
Vol 8 (2) ◽  
pp. 173-183 ◽  
Author(s):  
Magdalena T. Tosteson ◽  
Michael P. Caulfield ◽  
Jay J. Levy ◽  
Michael Rosenblatt ◽  
Daniel C. Tosteson
Keyword(s):  
Parathyroid Hormone ◽  
Ion Channels ◽  
Lipid Bilayers ◽  
Signal Sequence ◽  
Signal Peptides ◽  
Signal Sequences ◽  
Amphipathic Peptides ◽  
Voltage Dependent ◽  
Pro Region ◽  
Potential Signal

We have used the chemically synthesized sequence of pre-pro-parathyroid hormone and several of its analogues to test the notion that the capacity of amphipathic peptides to aggregate in membranes and form ion-permeable channels correlates with their ability to function as signal sequences for secreted proteins. We found that pre-pro-parathyroid hormone (the signal sequence and pro-region of parathyroid hormone (M)), as well as some of its analogues, forms aggregates of monomers which are ion-permeable. The ion-permeable aggregates (2–3 monomers) formed by (M) are voltage-dependent and are more permeable for cations than for anions. The compounds which formed ion channels in bilayers also acted as potential signal sequences. We conclude that the ability of peptides to form ion-permeable pathways in bilayers may be correlated to their ability to function as signal peptides.

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