Functional domains of template-activating factor-I as a protein phosphatase 2A inhibitor

Shoko Saito, Mary Miyaji-Yamaguchi, Tae Shimoyama, Kyosuke Nagata

Research output: Contribution to journalArticlepeer-review

54 Citations (Scopus)

Abstract

Template-Activating Factor-I (TAF-I) α and β, chromatin remodeling factors, were identified as the stimulatory factor for replication of the adenovirus DNA complexed with viral basic core proteins. Recently, two cellular inhibitors for protein phosphatase 2A (PP2A) have been isolated. One of these inhibitors, designated I2(PP2A), is a truncated version of TAF-Iβ. Here, it is shown using recombinant TAF-I proteins that both TAF-Iα and β have the PP2A inhibitor activity. The N-terminal region but not the C-terminal acidic region, the latter of which is essential for the chromatin remodeling activity, is shown to be required for the PP2A inhibitor activity. Roles of TAF-Iα- and β-specific regions, the C-terminal acidic region, and other regions of TAF-I for the PP2A inhibitor activity are also discussed.

Original languageEnglish
Pages (from-to)471-475
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume259
Issue number2
DOIs
Publication statusPublished - Jun 7 1999
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint

Dive into the research topics of 'Functional domains of template-activating factor-I as a protein phosphatase 2A inhibitor'. Together they form a unique fingerprint.

Cite this