Related Experiment Video
Updated: Jul 11, 2026
07:55
Detection of Homologous Recombination Intermediates via Proximity Ligation and Quantitative PCR in Saccharomyces cerevisiae
Published on: September 11, 2022
Rad52 multimerization is important for its nuclear localization in Saccharomyces cerevisiae
Iben Plate1, Line Albertsen, Michael Lisby
1Center for Microbial Biotechnology, BioCentrum-DTU, Technical University of Denmark, Bldg. 223, DK-2800 Kgs. Lyngby, Denmark.
DNA Repair
|September 25, 2007
Summary
Rad52 protein nuclear import in yeast relies on a weak nuclear localization signal (NLS). Multiple NLS(Rad52) sites in Rad52 complexes enhance nuclear transport for DNA repair.
Area of Science:
- Molecular Biology
- Cell Biology
- Genetics
Background:
- Rad52 is crucial for homologous recombination and DNA double-strand break repair in Saccharomyces cerevisiae.
- Rad52's nuclear import mechanism was previously unknown.
- Rad52 possesses multiple domains for DNA and protein interactions.
Purpose of the Study:
- To elucidate the mechanism of Rad52 nuclear import in S. cerevisiae.
- To identify the specific sequences responsible for Rad52 nuclear localization.
Main Methods:
- Sequence analysis and mutagenesis of Rad52.
- Assessment of nuclear localization of Rad52 variants.
- Analysis of DNA repair proficiency.
Main Results:
- A single pat7 type nuclear localization signal (NLS) in Rad52 was identified.
- This NLS is essential for nuclear import but not for MMS-induced DNA repair.
- Monomeric Rad52 with the NLS shows weak nuclear localization, while multimeric Rad52 complexes are efficiently imported.
Conclusions:
- The additive effect of multiple NLS(Rad52) sequences within Rad52 ring structures ensures efficient nuclear localization.
- This mechanism is vital for Rad52's role in DNA repair pathways.
Related Concept Videos
01:57Protein Complexes with Interchangeable Parts
Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
01:28Yeast Signaling
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...
02:53Conservative Site-specific Recombination and Phase Variation
Because the DNA segments are cut and reorganized in a direction-specific manner, site-specific recombination has emerged as an efficient genetic engineering technique. Flippase and Cyclization recombinases or Flp and Cre, respectively, are two members of the tyrosine recombinase family derived from bacteriophages, that are used to mediate site-specific DNA insertions, deletions, and targeted expression of proteins in mammalian cell lines.
The recognition sites for Cre recombinase called LoxP...
The recognition sites for Cre recombinase called LoxP...