High impact information on DGA1

• Using a dga1lro1are1are2 quadruple mutant transformed with plasmids bearing inducible DGA1, LRO1, or ARE2 we demonstrate that TAG synthesis contributes more efficiently to lipid particle proliferation than synthesis of STE [1].
• In vitro microsomal assays verified that DGA1 and ARE2 mediate acyl-CoA:diacylglycerol acyltransferase reactions [2].
• The DGA1 gene determines a second triglyceride synthetic pathway in yeast [2].
• In a dga1 deletion strain, the DAGAT activity in lipid particles is dramatically reduced, whereas the activity in microsomes is affected only to a minor extent [3].
• With the exception of Dga1p, whose activity is partially localized to lipid particles, TAG and STE forming enzymes are restricted to the endoplasmic reticulum [4].

Biological context of DGA1

• Acylation of DAG to yield TAG is catalyzed mainly by the two yeast proteins Dga1p and Lro1p, which utilize acyl-CoA or phosphatidylcholine, respectively, as acyl donors [5].

Other interactions of DGA1

• The contribution of two lipid particle-associated proteins (namely Tgl1p and Dga1p) to this process is described [6].

References