Two different cellular redox systems regulate the DNA-binding activity of the p50 subunit of NF-κB in vitro

Mitomo Katsuyuki, Nakayama Kohzo, Fujimoto Kotaro, Sun Xiangao, Seki Shuji, Ken-ichi Yamamoto

Research output: Contribution to journalArticle

122 Citations (Scopus)

Abstract

The NF-κB/Rel/Dorsal (NRD) transcription factor family binds target DNA sequences through their conserved N-terminal basic region that contains a single cysteine residue flanked by basic residues. This cysteine residue plays a critical role in the regulation of the DNA-binding activity of NRD members, since chemical modifications of this residue modulate the DNA-binding activity of NRD members. Here we show that cellular factors regulate the DNA-binding activity of NRD members in vitro by reduction-oxidation (redox) mechanisms. Two cellular redox systems, thioredoxin/thioredoxin reductase and apurinic/apyrimidinic endonuclease (also called Redox factor-1), independently, as well as, synergistically stimulate the DNA-binding activity of bacterially synthesized (recombinant) p50, one of the subunits of NF-κB that is a major NRD factor inducible in various types of cells. Since the mutation of the conserved residue (Cys61) in the N-terminal basic region of p50 impairs the stimulation of p50 DNA-binding activity by these redox factors, the regulation of p50 DNA-binding activity by these redox factors is mediated through this cysteine residue. It is, therefore, possible that these two cellular redox systems could play independent, as well as synergistic roles in the regulation of NF-κB functions in vivo through the redox control of their DNA-binding activity.

Original languageEnglish
Pages (from-to)197-203
Number of pages7
JournalGene
Volume145
Issue number2
DOIs
Publication statusPublished - Aug 5 1994
Externally publishedYes

Fingerprint

DNA
Cysteine
DNA-(Apurinic or Apyrimidinic Site) Lyase
Thioredoxin-Disulfide Reductase
Thioredoxins
In Vitro Techniques
Oxidation-Reduction
Transcription Factors
Mutation

Keywords

  • DNA repair enzyme
  • inflammation
  • reactive oxygene
  • Redox regulation

ASJC Scopus subject areas

  • Genetics

Cite this

Two different cellular redox systems regulate the DNA-binding activity of the p50 subunit of NF-κB in vitro. / Katsuyuki, Mitomo; Kohzo, Nakayama; Kotaro, Fujimoto; Xiangao, Sun; Shuji, Seki; Yamamoto, Ken-ichi.

In: Gene, Vol. 145, No. 2, 05.08.1994, p. 197-203.

Research output: Contribution to journalArticle

Katsuyuki, Mitomo ; Kohzo, Nakayama ; Kotaro, Fujimoto ; Xiangao, Sun ; Shuji, Seki ; Yamamoto, Ken-ichi. / Two different cellular redox systems regulate the DNA-binding activity of the p50 subunit of NF-κB in vitro. In: Gene. 1994 ; Vol. 145, No. 2. pp. 197-203.
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