PCCX1, a novel DNA-binding protein with PHD finger and CXXC domain, is regulated by proteolysis

Tadahiro Fujino, Mayumi Hasegawa, Shinsuke Shibata, Taishiro Kishimoto, Shin Ichiro Imai, Toshiya Takano

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

We identified a novel gene PCCX1 that encoded a nuclear protein carrying a PHD finger, a CXXC domain, and an acidic region. The CXXC domain was found to be sufficient for binding to DNA. The acidic region exhibited a high transactivation ability, but the full-length protein was inactive due to regions which inhibited the acidic region, including the C-terminal region. We examined the expression of PCCX1 during cellular aging and immortalization of SV40-transformed human fibroblasts. PCCX1 mRNA was expressed constitutively through stages of cellular aging and immortalization, but at the protein level, a shorter form lacking the C-terminal region appeared as the cells approached crisis. These results suggested that PCCX1 was activated by proteolytic cleavage, which removed the C-terminal inhibitory region. (C) 2000 Academic Press.

Original languageEnglish
Pages (from-to)305-310
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume271
Issue number2
DOIs
Publication statusPublished - 2000 May 10

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'PCCX1, a novel DNA-binding protein with PHD finger and CXXC domain, is regulated by proteolysis'. Together they form a unique fingerprint.

  • Cite this