Molecular cloning of nucleobindin, a novel DNA-binding protein that contains both a signal peptide and a leucine zipper structure

Keiji Miura, Koiti Titani, Yoshikazu Kurosawa, Yoshiyuki Kanai

Research output: Contribution to journalArticle

102 Citations (Scopus)

Abstract

We have previously reported that KML1-7 cells cloned from a lupus-prone MRL/1 mouse produced a soluble factor that preferentially expanded anti-DNA antibody production across the H-2 barrier. We purified this factor, a 55 kD protein that we termed nucleobindin (Nuc), and obtained its cDNA clone. Although the gene for Nuc encodes a signal peptide and, in fact, Nuc was identified as a secreted protein, Nuc had a DNA binding property. The putative polypeptide predicted from the cDNA sequence featured a signal peptide, a leucine zipper structure and a basic amino acid-rich region. The DNA-binding property of Nuc was destroyed by deletion of either the leucine zipper structure or the basic amino acid-rich region. The amino acid sequences of Nuc are highly conserved between mouse and human. We discuss the possible role of Nuc in autoimmunity.

Original languageEnglish
Pages (from-to)375-380
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume187
Issue number1
DOIs
Publication statusPublished - 31-08-1992

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'Molecular cloning of nucleobindin, a novel DNA-binding protein that contains both a signal peptide and a leucine zipper structure'. Together they form a unique fingerprint.

Cite this