A human gene coding for a membrane-associated nucleic acid-binding protein

Don C. Siess, Colleen T. Vedder, Louise S. Merkens, Toshiko Tanaka, Alison C. Freed, Sharon L. McCoy, Michael C. Heinrich, Mark E. Deffebach, Robert M. Bennett, Steven H. Hefeneider

Research output: Contribution to journalArticlepeer-review

49 Scopus citations


Studies to clone a cell-surface DNA-binding protein involved in the binding and internalization of extracellular DNA have led to the isolation of a gene for a merebrane-associated nucleic acid-binding protein (MNAB). The full-length cDNA is 4.3 kilobases with an open reading frame of 3576 base pairs encoding a protein of ~130 kDa (GenBank accession numbers AF255303 and AF255504). The MNAB gene is on human chromosome 9 with wide expression in normal tissues and tumor cells. A C3HC4 RING finger and a CCCH zinc finger have been identified in the amino-terminal half of the protein. MNAB bound DNA (K(D) ~4 nM) and mutagenesis of a single conserved amino acid in the zinc finger reduced DNA binding by 50%. A potential transmembrane domain exists near the carboxyl terminus. Antibodies against the amino-terminal half of the protein immunoprecipitated a protein of molecular mass ~150 kDa and reacted with cell surfaces. The MNAB protein is membrane-associated and primarily localized to the perinuclear space, probably to the endoplasmic reticulum or trans-Golgi network. Characterization of the MNAB protein as a cell-surface DNA-binding protein, critical in binding and internalization of extracellular DNA, awaits confirmation of its localization to cell surfaces.

Original languageEnglish (US)
Pages (from-to)33655-33662
Number of pages8
JournalJournal of Biological Chemistry
Issue number43
StatePublished - Oct 27 2000

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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