| Autor: |
Weselake, R. J., Nykiforuk, C. L., Laroche, A., Patterson, N. A., Wiehler, W. B., Szarka, S. J., Moloney, M. M., Tari, L. W., Derekh, U. |
| Zdroj: |
Biochemical Society Transactions; December 2000, Vol. 28 Issue: 6 p684-686, 3p |
| Abstrakt: |
The expression of diacylglycerol acyltransferase (DGAT, EC 2.3.1.20) with predicted molecular mass of 56.9. kDa (BnDGAT1) was examined using microspore-derived cell suspension cultures of oilseed rape (Brassica napus L. cv Jet Neuf). As well, a recombinant histidine-tagged N-terminal fragment of BnDGAT1 [BnDGAT1(1–116)His6], which was relatively hydrophilic, was partially characterized. A temporal increase in DGAT activity occurred within a 24 h period following transfer of cells from 6% (w/v) sucrose to 14% (w/v) sucrose. Western blotting indicated that the abundance of BnDGAT1 protein was closely correlated with DGAT activity. BnDGAT1 mRNA also exhibited a temporal increase within the 24 h period following transfer of cells into higher sucrose concentrations, but the transcript level was not closely associated with DGAT activity as BnDGAT1 protein. The fragment BnDGAT1(1–116)His6, interacted with [1-14C] oleoyl-CoA, suggesting that the N-terminal region of BnDGAT1 may have a role in binding cellular acyl-CoA. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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