Cloning and characterization of a novel RING-B-box-coiled-coil protein with apoptotic function

J Biol Chem. 2003 Jul 4;278(27):25046-54. doi: 10.1074/jbc.M303438200. Epub 2003 Apr 10.

Abstract

We have identified a novel RING-B-box-coiled-coil (RBCC) protein (MAIR for macrophage-derived apoptosis-inducing RBCC protein) that consists of an N-terminal RING finger, followed by a B-box zinc finger, a coiled-coil domain, and a B30.2 domain. MAIR mRNA was expressed widely in mouse tissues and was induced by macrophage colony-stimulating factor in murine peritoneal and bone marrow macrophages. MAIR protein initially showed a granular distribution predominantly in the cytoplasm. The addition of zinc to transfectants containing MAIR cDNA as part of a heavy metal-inducible vector caused apoptosis of the cells characterized by cell fragmentation; a reduction in mitochondrial membrane potential; activation of caspase-7, -8, and -9, but not caspase-3; and DNA degradation. We also found that the RING finger and coiled-coil domains were required for MAIR activity by analysis with deletion mutants.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Apoptosis / genetics*
  • Apoptosis Regulatory Proteins
  • Base Sequence
  • Carrier Proteins / genetics*
  • Cloning, Molecular
  • Mice
  • Molecular Sequence Data
  • Mutation
  • Organ Specificity
  • Proteins / genetics*
  • Sequence Alignment
  • Zinc Fingers

Substances

  • Apoptosis Regulatory Proteins
  • Carrier Proteins
  • Proteins
  • TRIM35 protein, human

Associated data

  • GENBANK/AB060155