Ståhl Ulf, Stålberg Kjell, Stymne Sten, Ronne Hans
Department of Plant Biology and Forest Genetics, Swedish University of Agricultural Sciences, Uppsala, Sweden.
FEBS Lett. 2008 Jan 23;582(2):305-9. doi: 10.1016/j.febslet.2007.12.020. Epub 2007 Dec 26.
The budding yeast ALE1 gene encodes a lysophospholipid acyltransferase (LPLAT) with broad specificity. We show that yeast LPLAT (ScLPLAT) belongs to a distinct protein family that includes human MBOAT1, MBOAT2, MBOAT4, and several closely related proteins from other eukaryotes. We further show that two plant proteins within this family, the Arabidopsis proteins AtLPLAT1 and AtLPLAT2, possess lysophospholipid acyltransferase activities similar to ScLPLAT. We propose that other members of this protein family, which we refer to as the LPLAT family, also are likely to possess LPLAT activity. Finally, we show that ScLPLAT differs from the specific lysophosphatidic acid acyltransferase that is encoded by SLC1 in that it cannot efficiently use lysophosphatidic acid produced by acylation of glycerol-3-phosphate in vitro.
出芽酵母ALE1基因编码一种具有广泛特异性的溶血磷脂酰基转移酶（LPLAT）。我们发现酵母LPLAT（ScLPLAT）属于一个独特的蛋白质家族，该家族包括人类MBOAT1、MBOAT2、MBOAT4以及来自其他真核生物的几种密切相关的蛋白质。我们进一步表明，该家族中的两种植物蛋白，即拟南芥蛋白AtLPLAT1和AtLPLAT2，具有与ScLPLAT相似的溶血磷脂酰基转移酶活性。我们推测这个我们称为LPLAT家族的蛋白质家族的其他成员也可能具有LPLAT活性。最后，我们发现ScLPLAT与由SLC1编码的特定溶血磷脂酸酰基转移酶不同，因为它在体外不能有效地利用由甘油-3-磷酸酰化产生的溶血磷脂酸。
