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Precise mapping of the tms1 binding site on p53
Abstract:
Originally identified as multicopy suppressor of a lethal growth arrest caused by expression of a tumour mutant cDNA of p53 in fission yeast the tms1 gene product was found to form stable complexes with p53 in yeast. By using purified recombinant proteins multimeric complexes of tms1 and p53 could be demonstrated and recently the p53 binding site on the tms1 protein was established to the sequence YYITTEDFCT (aa 116-125) in the vicinity of a well conserved cell division motif. Here we report the precise mapping of the tms1 binding site on the p53 protein to the sequence LQIRGRERFE (aa 330-339) which defines a new functional domain on the p53 protein.
Insights
The tms1 protein binds to a new functional domain on p53 (tumor protein 53). This interaction, involving specific amino acid sequences, was precisely mapped using purified recombinant proteins in yeast.
Area of Science:
- Molecular biology
- Yeast genetics
- Protein-protein interactions
Background:
- The tms1 gene was initially identified as a suppressor of growth arrest caused by a mutant p53 tumor gene in fission yeast.
- The tms1 protein forms stable complexes with p53 in yeast.
- A previously identified p53 binding site on tms1 is located near a conserved cell division motif.
Purpose of the Study:
- To precisely map the binding site of tms1 on the p53 protein.
- To identify a new functional domain on p53.
Main Methods:
- Using purified recombinant proteins to demonstrate multimeric complexes of tms1 and p53.
- Precise mapping of the tms1 binding site on p53 using protein sequence analysis.
Main Results:
- The tms1 protein binds to the specific sequence LQIRGRERFE (amino acids 330-339) on the p53 protein.
- This binding region defines a novel functional domain on p53.
Conclusions:
- The precise mapping of the tms1 binding site on p53 reveals a new functional domain.
- Understanding these interactions is crucial for comprehending p53 regulation and function.