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Protein Dynamics in Living Cells

Protein Dynamics in Living Cells

Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...

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Related Experiment Video

Updated: May 4, 2026

Fluorescence Recovery after Photobleaching of Yellow Fluorescent Protein Tagged p62 in Aggresome-like Induced Structures

Fluorescence Recovery after Photobleaching of Yellow Fluorescent Protein Tagged p62 in Aggresome-like Induced Structures

Published on: March 26, 2019

Rad52 protein function study by fluorescence tagging.

Gabriela Bordeianu¹, Elena Petrescu-Danila, Didona Ungureanu

¹Faculty of Medicine, University of Medicine and Pharmacy "Grigore T. Popa" - Iasi.

Revista Medico-Chirurgicala a Societatii De Medici Si Naturalisti Din Iasi

|December 18, 2013

Summary

This summary is machine-generated.

This study successfully tagged the Rad22 protein in Schizosaccharomyces pombe using a novel method. The tagged Rad22 protein was observed to form foci in response to DNA damage, aiding in DNA repair research.

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Area of Science:

Molecular Biology
Genetics
Cell Biology

Background:

Rad52 protein is crucial for DNA repair via homologous recombination in eukaryotes.
Human Rad52 shares functions with BRCA2, supporting cell survival when BRCA1-BRCA2 mediated recombination is absent.
Further investigation into Rad52 functions and localization is needed.

Purpose of the Study:

To develop and validate a method for tagging the Rad22 protein, a homolog of human Rad52, in Schizosaccharomyces pombe.
To analyze the intracellular localization and behavior of tagged Rad22 protein under DNA-damaging conditions.

Main Methods:

Utilized Crerecombinase-mediated cassette exchange (RMCE) with the pAW8 plasmid for C-terminal yEGFP tagging of Rad22.
Analyzed the resulting S. pombe strain using fluorescence microscopy.
Confirmed the presence and integrity of tagged Rad22 via Western-Blot analysis.

Main Results:

Successfully generated a C-termini yEGFP tagged Rad22 protein in S. pombe.
Observed Rad22 foci formation in response to DNA damaging agents: camptothecin, methyl methanesulfonate, and hydroxyurea.
Demonstrated the efficiency of the RMCE method for protein tagging.

Conclusions:

The RMCE method is effective for tagging Rad22 in S. pombe.
Tagged Rad22 exhibits localization dynamics indicative of its role in DNA repair pathways.
This tagged Rad22 provides a valuable tool for studying DNA repair mechanisms in S. pombe.