Nucleotide binding of the C-terminal domains of the major histocompatibility complex-encoded transporter expressed in Drosophila melanogaster cells

FEBS Lett. 1994 Aug 22;350(2-3):337-41. doi: 10.1016/0014-5793(94)00806-x.

Abstract

The C-terminal domains of the mouse transporter associated with antigen processing (TAP) were expressed as soluble proteins in Drosophila melanogaster cells and labeled by [alpha-32P]8-azido-ATP after UV-irradiation. The relative potencies of the nucleotides in preventing azido-ATP labeling were in the order of ATP > GTP > CTP > ITP > UTP for both the TAP1 and TAP2 C-terminal domains, suggesting ATP to be the natural substrate of the transporter. Our data provide the first evidence that the individual C-terminal domain of either TAP1 or TAP2 can be expressed as a functional ATP-binding protein.

MeSH terms

  • ATP Binding Cassette Transporter, Subfamily B, Member 2
  • ATP Binding Cassette Transporter, Subfamily B, Member 3
  • ATP-Binding Cassette Transporters*
  • Adenosine Triphosphate / metabolism*
  • Affinity Labels
  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Carrier Proteins / metabolism*
  • DNA Primers / chemistry
  • Drosophila melanogaster
  • Mice
  • Molecular Sequence Data
  • Photochemistry
  • Recombinant Proteins

Substances

  • ATP Binding Cassette Transporter, Subfamily B, Member 2
  • ATP Binding Cassette Transporter, Subfamily B, Member 3
  • ATP-Binding Cassette Transporters
  • Affinity Labels
  • Carrier Proteins
  • DNA Primers
  • Recombinant Proteins
  • TAP1 protein, human
  • Tap1 protein, mouse
  • Tap2 protein, mouse
  • TAP2 protein, human
  • Adenosine Triphosphate