In silico and in vitro characterization of mGBP4 splice variants

DNA Cell Biol. 2007 Dec;26(12):847-51. doi: 10.1089/dna.2007.0637.

Abstract

In a systematic approach to identify interferon-gamma (IFN-gamma)-regulated host effector molecules, we found several members of the 65 kDa guanylate-binding proteins (GBPs) highly upregulated. During extensive characterization of these guanosine triphosphatases (GTPases), we identified discrepancies between the cloned and published sequences of the murine GTPase mGBP4. Two splice variants of mGBP4 could be detected. One variant led to a premature stop codon after 312 bp. The second variant resulted in a transcript with a disrupted G2 domain and was deposited as mGBP4.1 to the GenBank. Interestingly, only mGBP4, not mGBP4.1 mRNA, was highly upregulated in mice after infection with Listeria monocytogenes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alternative Splicing*
  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cell Line
  • Codon, Nonsense
  • DNA Primers / genetics
  • DNA, Complementary / genetics
  • GTP-Binding Proteins / chemistry
  • GTP-Binding Proteins / genetics*
  • Listeriosis / genetics
  • Listeriosis / metabolism
  • Mice
  • Mice, Inbred C57BL
  • Molecular Sequence Data
  • Protein Structure, Tertiary
  • RNA, Messenger / genetics
  • RNA, Messenger / metabolism
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Transfection

Substances

  • Codon, Nonsense
  • DNA Primers
  • DNA, Complementary
  • RNA, Messenger
  • Recombinant Proteins
  • GTP-Binding Proteins
  • Mpa2 protein, mouse

Associated data

  • GENBANK/EF494423
  • GENBANK/EF494424