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Complex formation between proteins encoded by the ski gene family
1Laboratory of Molecular Genetics, Tsukuba Life Science Center, The Institute of Physical and Chemical Research (RIKEN), Ibaraki, Japan.
The Journal of Biological Chemistry
|June 25, 1993
Summary
The c-Ski proto-oncogene protein forms complexes with itself and SnoN, potentially involving leucine zipper structures. This self-association and interaction with SnoN may be crucial for c-Ski
Area of Science:
- Molecular Biology
- Cell Biology
- Oncogene Research
Background:
- The function and biochemical properties of the c-Ski proto-oncogene product (c-Ski) remain largely unknown.
- c-Ski is localized in the cell nucleus and requires association with other proteins for DNA binding.
Purpose of the Study:
- To identify proteins that form complexes with c-Ski.
- To elucidate the biochemical properties and potential self-association of c-Ski.
Main Methods:
- Screening of a lambda gt11 cDNA library using biotinylated Ski.
- Protein cross-linking and protein blot analysis to confirm complex formation.
- Analysis of carboxyl-terminal regions of Ski and SnoN for complex formation domains.
Main Results:
- Isolation of clones encoding c-Ski and its related protein, SnoN, indicating complex formation.
- Confirmation of trimerization between c-Ski and SnoN via protein cross-linking and blot analysis.
- Identification of the carboxyl-terminal 1/5 regions of Ski and SnoN as essential for complex formation, featuring homologous sequences and leucine zipper-like structures.
Conclusions:
- c-Ski can form complexes with itself and with SnoN.
- Leucine zipper-like structures within the carboxyl-terminal regions likely mediate this trimerization.
- Complex formation involving c-Ski, SnoN, and other proteins may be critical for c-Ski's nuclear function.