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The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
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Immunoprecipitation, or IP, is a widely used technique that employs protein-antibody interactions to isolate proteins or protein complexes in their native state for studying protein-protein interactions, quaternary structures, or supramolecular complexes. Various modifications of the technique, including chromatin IP, cross-linking IP, and fluorescence IP, are commonly used.
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The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
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Studying Protein Function and the Role of Altered Protein Expression by Antibody Interference and Three-dimensional Reconstructions
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Conditional Protein Rescue by Binding-Induced Protective Shielding.

Andrew S Gaynor1, Wilfred Chen1

  • 1Department of Chemical and Biomolecular Engineering, University of Delaware, Newark, Delaware 19716, United States.

ACS Synthetic Biology
|October 7, 2020
PubMed
Summary
This summary is machine-generated.

We developed conditional protein rescue (CPR) to control protein activity using protein inputs. This synthetic biology tool enables precise cellular control and can distinguish cancer cells for diagnostics.

Keywords:
cancerprodrugsprotein engineeringprotein−protein interactionssynthetic biology

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Area of Science:

  • Synthetic biology
  • Molecular and cell biology
  • Biotechnology

Background:

  • Conventional gene-level circuits offer cellular control, but protein-level circuits provide an additional regulatory layer.
  • Existing methods for protein control are limited in scope and generalizability.

Purpose of the Study:

  • To develop a novel technology for conditional protein rescue (CPR) from proteasomal degradation.
  • To establish a generalizable platform for executing diverse protein-level synthetic biology circuits.

Main Methods:

  • Engineered a system where a target protein is fused to a degron tag and an affinity sensor domain (nanobodies).
  • Utilized protein inputs as masking agents to conditionally rescue proteins from degradation.
  • Demonstrated CPR's utility in distinguishing cancer cells using the human papillomavirus (HPV) E7 protein as a marker.

Main Results:

  • Successfully implemented conditional protein rescue (CPR) technology.
  • Showcased the use of nanobodies as versatile affinity sensors for protein-level circuit design.
  • Validated CPR's ability to differentiate cancer cells from healthy cells based on HPV E7 expression.

Conclusions:

  • Conditional protein rescue (CPR) provides a powerful and modular framework for synthetic protein circuits.
  • This technology enables complex Boolean logic operations at the protein level.
  • CPR offers a scalable platform with broad applications in synthetic biology and diagnostics.