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Yeast Signaling01:28

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Yeasts are single-celled organisms, but unlike bacteria, they are eukaryotes (cells with a nucleus). Cell signaling in yeast is similar to signaling in other eukaryotic cells. A ligand, such as a protein or a small molecule released from a yeast cell, attaches to a receptor on the cell surface. The binding stimulates second-messenger kinases to activate or inactivate transcription factors that further regulate gene expression. Many of the yeast intracellular signaling cascades have similar...
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Protein Engineering by Yeast Surface Display
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A platform for constructing, evaluating, and screening bioconjugates on the yeast surface.

James A Van Deventer1,2,3, Doris N Le2,3, Jessie Zhao2,3

  • 1Chemical and Biological Engineering Department, Tufts University, 4 Colby Street Room 148, Medford, MA 02155, United States of America.

Protein Engineering, Design & Selection : PEDS
|August 13, 2016
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Summary
This summary is machine-generated.

Yeast display enables the site-specific incorporation of noncanonical amino acids (ncAAs) into proteins. This facilitates high-throughput screening of chemically modified polypeptides for therapeutic discovery.

Keywords:
antibodiesclick chemistryhigh throughput screeningnoncanonical amino acidsyeast display

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Biotechnology

Background:

  • Protein display technologies and noncanonical amino acids (ncAAs) offer powerful tools for biological research.
  • Existing platforms like mRNA, phage, and E. coli display have limitations in evaluating ncAA conjugation and stability.
  • There is a need for advanced platforms for high-throughput screening of modified proteins.

Purpose of the Study:

  • To develop and validate an ncAA-compatible yeast display platform.
  • To enable site-specific introduction and modification of ncAAs in displayed proteins.
  • To facilitate high-throughput screening and characterization of chemically modified polypeptides.

Main Methods:

  • Utilized ncAA-compatible yeast display for protein engineering.
  • Introduced ncAAs site-specifically into yeast-displayed proteins.
  • Performed robust chemical modifications at azide-containing residues.
  • Quantitatively evaluated protein conjugates directly on the yeast surface.
  • Implemented screening for enrichment of modified constructs with genotype-phenotype linkage.

Main Results:

  • Demonstrated the feasibility of ncAA incorporation and modification using yeast display.
  • Showcased the platform's ability to evaluate conjugation chemistry and stability.
  • Achieved selective enrichment of chemically modified protein libraries.
  • Maintained essential genotype-phenotype linkage throughout the screening process.

Conclusions:

  • ncAA-compatible yeast display is a robust platform for high-throughput characterization and screening.
  • This approach overcomes limitations of existing display technologies for modified proteins.
  • The platform is well-suited for therapeutic lead discovery and other biological applications.