P53 FORMS TIGHT COMPLEXES WITH TMS1 OF FISSION YEAST

  • Authors:
    • P WAGNER
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  • Published online on: April 1, 1994     https://doi.org/10.3892/ijo.4.4.987
  • Pages: 987-992
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Abstract

Recently we reported the isolation of tms1, an extragenic multicopy suppressor of a human p53 His273 tumour mutant-induced growth arrest in fission yeast (Wagner et al: Eur J Biochem 217: 731-736, 1993). tms1 encodes a putative dehydrogenase. We demonstrate direct interaction of p53 with the tms1 protein in vivo. Using p53-specific or tms1-specific polyclonal antibodies, coprecipitation of p53 His273 or p53 wild type with tms1 protein could be shown with extracts from transformed yeast cells. Recombinant purified C-terminal peptide of p53 and tms1 protein were used to demonstrate specific complex formation and to map the interaction to the C-terminus of p53 in vitro by west-Western blot and HPLC analysis.

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April 1994
Volume 4 Issue 4

Print ISSN: 1019-6439
Online ISSN:1791-2423

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Spandidos Publications style
WAGNER P: P53 FORMS TIGHT COMPLEXES WITH TMS1 OF FISSION YEAST. Int J Oncol 4: 987-992, 1994
APA
WAGNER, P. (1994). P53 FORMS TIGHT COMPLEXES WITH TMS1 OF FISSION YEAST. International Journal of Oncology, 4, 987-992. https://doi.org/10.3892/ijo.4.4.987
MLA
WAGNER, P."P53 FORMS TIGHT COMPLEXES WITH TMS1 OF FISSION YEAST". International Journal of Oncology 4.4 (1994): 987-992.
Chicago
WAGNER, P."P53 FORMS TIGHT COMPLEXES WITH TMS1 OF FISSION YEAST". International Journal of Oncology 4, no. 4 (1994): 987-992. https://doi.org/10.3892/ijo.4.4.987