Abstract
AtSUT2 was found to be a low-affinity sucrose transporter (K(M) = 11.7 mM at pH 4). Chimeric proteins between AtSUT2 and the high-affinity StSUT1 were constructed in which the extended N-terminus and central loop of AtSUT2 were exchanged with those domains of StSUT1 and vice versa. Chimeras containing the N-terminus of AtSUT2 showed significantly lower affinity for sucrose compared to chimeras containing the N-terminus of StSUT1. The results indicate a significant function of the N-terminus but not the central cytoplasmic loop in determining substrate affinity. Expression of AtSUT2 in major veins of source leaves and in flowers is compatible with a role as a second low-affinity sucrose transporter or as a sucrose sensor. (C) 2000 Federation of European Biochemical Societies.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 189-194 |
| Number of pages | 6 |
| Journal | FEBS Letters |
| Volume | 485 |
| Issue number | 2-3 |
| DOIs | |
| State | Published - Nov 24 2000 |
Keywords
- Protein chimera
- Sucrose sensor
- Sucrose transporter