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 [α-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.
Original language | English (US) |
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Pages (from-to) | 337-341 |
Number of pages | 5 |
Journal | FEBS Letters |
Volume | 350 |
Issue number | 2-3 |
DOIs | |
State | Published - Aug 22 1994 |
Externally published | Yes |
Keywords
- ATP-binding cassette transporter
- Antigen presentation
- Major histocompatibility complex
- Traffic ATP-ase
- Transporter associated with antigen processing
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology