Related Experiment Videos
ALL-1 interacts with unr, a protein containing multiple cold shock domains
D Leshkowitz1, O Rozenblatt, T Nakamura
1Department of Molecular Cell Biology, Weizmann Institute of Science, Rehovot, Israel.
Oncogene
|November 7, 1996
Summary
The ALL-1 gene, implicated in acute leukemia, interacts with the unr gene product. This interaction, involving cold shock domains, suggests unr may mediate ALL-1
Area of Science:
- Molecular Biology
- Genetics
- Cancer Research
Background:
- The ALL-1 gene is crucial in human acute leukemia, often altered by chromosomal translocations or duplications.
- ALL-1 is the human counterpart of Drosophila trithorax, regulating key developmental genes.
- The large ALL-1 protein (3968 amino acids) is expected to interact with numerous other proteins.
Purpose of the Study:
- To identify proteins that interact with the N-terminal region of the ALL-1 gene product.
- To investigate the role of the unr gene product in ALL-1 protein interactions.
Main Methods:
- Yeast two-hybrid screening was employed to detect protein-protein interactions.
- In vitro binding assays and co-immunoprecipitation were used for confirmation.
- Studies involved overexpressing relevant protein segments in COS cells.
Main Results:
- The unr gene product was identified as an interacting protein with the N-terminal segment of ALL-1.
- The unr protein contains multiple cold shock domains (CSDs), a known nucleic acid-binding motif.
- Interaction required specific regions of unr, including two CSDs and intervening sequences.
Conclusions:
- The unr gene product physically interacts with the ALL-1 protein.
- The presence of CSDs in unr suggests a potential role in mediating ALL-1's interaction with nucleic acids (DNA or RNA).
- This interaction may be significant in the biological functions of ALL-1, including its role in leukemia.