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J. Biol. Chem., Vol. 276, Issue 42, 38862-38869, October 19, 2001
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From the Calgene Campus/Monsanto, Davis, California 95616
Acyl CoA:diacylgycerol acyltransferase (EC
2.3.1.20; DGAT) catalyzes the final step in the production of
triacylglycerol. Two polypeptides, which co-purified with DGAT
activity, were isolated from the lipid bodies of the oleaginous fungus
Mortierella ramanniana with a procedure consisting of dye
affinity, hydroxyapatite affinity, and heparin chromatography. The two
enzymes had molecular masses of 36 and 36.5 kDa, as estimated by gel
electrophoresis, and showed a broad activity maximum between pH 6 and
8. Based on partial peptide sequence information, polymerase chain
reaction techniques were used to obtain full-length cDNA sequences
encoding the purified proteins. Expression of the cDNAs in insect
cells conferred high levels of DGAT activity on the membranes isolated
from these cells. The two proteins share 54% homology with each other
but are unrelated to the previously identified DGAT gene family
(designated DGAT1), which is related to the acyl CoA:cholesterol
acyltransferase gene family, or to any other gene family with ascribed
function. This report identifies a new gene family, including members
in fungi, plants and animals, which encode enzymes with DGAT function.
To distinguish the two unrelated families we designate this new class DGAT2 and refer to the M. ramanniana genes as
MrDGAT2A and MrDGAT2B.
DGAT2 Is a New Diacylglycerol Acyltransferase Gene Family
PURIFICATION, CLONING, AND EXPRESSION IN INSECT CELLS OF TWO
POLYPEPTIDES FROM MORTIERELLA RAMANNIANA WITH DIACYLGLYCEROL
ACYLTRANSFERASE ACTIVITY*
,
*
The costs of publication of this article were defrayed in
part by the payment of page charges. This article must therefore be
hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
To whom correspondence should be addressed: Calgene
Campus/Monsanto, 1920 Fifth St., Davis, CA 95616. E-mail:
kathy.lardizabal@monsanto.com.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) CAB04533 (CeDGAT2A), AAB04969 (CeDGAT2B), AAD45832 (CeDGAT2C), and BAB22105 (MmDGAT2).
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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