A novel factor associating with the upstream regulatory element of murine Hoxa-7 induces bacterial cell death

Mol Biol Rep. 2002 Dec;29(4):363-8. doi: 10.1023/a:1021228527097.

Abstract

In order to understand the function of a cDNA (c171) associated with the upstream regulatory region of the Hoxa-7, the cDNA was cloned into the pGEX-4T-1 vector to produce it as a GST fusion protein. The size of the fusion protein was determined to be 48-kilodalton (kDa). Sequence analysis revealed that a protein C171 contained one hydrophobic transmembrane domain in the N-terminal region and several putative phosphorylation and glycosylation sites. C171 protein inhibited the bacterial growth within 30 min after induction. The transmission electron microscopic examination revealed that the morphology of the cells expressing C171 was changed dramatically: i.e., unusually elongated phenotype compared with those of controls, and finally leading to a cell death. These results altogether indicate that a trace amount of C171 induces bacterial cell death.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cell Division
  • DNA-Binding Proteins / chemistry
  • DNA-Binding Proteins / genetics
  • DNA-Binding Proteins / metabolism*
  • Escherichia coli / cytology*
  • Escherichia coli / genetics*
  • Escherichia coli / growth & development
  • Escherichia coli / ultrastructure
  • Gene Expression
  • Glycosylation
  • Homeodomain Proteins / genetics*
  • Hydrophobic and Hydrophilic Interactions
  • Mice
  • Molecular Sequence Data
  • Molecular Weight
  • Phosphorylation
  • Protein Structure, Tertiary
  • Recombinant Fusion Proteins / chemistry
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / metabolism*
  • Response Elements / genetics*
  • Time Factors

Substances

  • DNA-Binding Proteins
  • Homeodomain Proteins
  • Recombinant Fusion Proteins

Associated data

  • GENBANK/AF335543