p53 amino acids 339-346 represent minimal p53 repression domain

Tse Ming Hong, Jeremy J.W. Cheni, Konan Peck, Pan Chyr Yang*, Cheng-Wen Wu

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

17 Scopus citations

Abstract

The p53 tumor suppressor protein functions as an activator and also as a repressor of gene transcription. Currently, the mechanism of transcriptional repression by p53 remains poorly understood. To help clarify this mechanism, we carried out studies designed to identify the minimal repression domain that inhibits p53 transcriptional activities. We found only eight amino acids (339-346) of the COOH-terminal domain (termed P53MRD) that possess activities of repression. The exact location of this minimal domain is on the E6-binding region, and it lacks the ability of tetramerization. P53MRD is able to repress the transcription of p53 while not affecting VP16. The mutants (amino acids M349P and F341D) of native p53 also lost transcriptional repression of the thymidine kinase chloramphenicol acetyltransferase promoter. These results suggest that this eight-amino acid element is required for the repression of p53.

Original languageEnglish
Pages (from-to)1510-1515
Number of pages6
JournalJournal of Biological Chemistry
Volume276
Issue number2
DOIs
StatePublished - 12 Jan 2001

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