Expression and properties of diacylglycerol acyltransferase from cell-suspension cultures of oilseed rape.

Abstract:

: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))His(6)], 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)His(6) interacted with [1-(14)C]oleoyl-CoA, suggesting that the N-terminal region of BnDGAT1 may have a role in binding cellular acyl-CoA.

journal_name

Biochem Soc Trans

authors

Weselake RJ,Nykiforuk CL,Laroche A,Patterson NA,Wiehler WB,Szarka SJ,Moloney MM,Tari LW,Derekh U

keywords:

subject

Has Abstract

pub_date

2000-12-01 00:00:00

pages

684-6

issue

6

eissn

0300-5127

issn

1470-8752

journal_volume

28

pub_type

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