Plasmodium falciparum dolichol phosphate mannose synthase represents a novel clade
- 作者：Hosam Shams-Eldin ; Cristiana Santos de Macedo ; Sebastian Niehus ; Caroline Dorn ; Jü ; rgen Kimmel ; Nahid Azzouz ; Ralph T. Schwarz
- 关键词：Malaria ; Plasmodium falciparum ; N-glycosylation ; Dolichol phosphate mannose synthases ; DPM ; GAL promoter ; Conditional lethal mutant ; Complementation
- 刊名：Biochemical and Biophysical Research Communications
- 出版年：2008
- 期刊代码：159_0006291x
- 类别：bio
- 出版时间：6 June 2008
- 卷：370
- 期：3
- 页码：388-393
- 文件大小：470 K
摘要
Dolichol phosphate mannose synthase (DPM) catalyzes the reaction between dolichol phosphate (Dol-P) and guanosine diphosphate mannose (GDP-Man) to form dolichol-phosphate-mannose (Dol-P-Man). This molecule acts as mannose donor for N-glycosylation and glycosylphosphatidylinositol (GPI) biosynthesis. The Plasmodium falciparum DPM1 (Pfdpm1) possesses a single predicted transmembrane region near the N-, but not the C-terminus. Here we show that the cloned Pfdpm1 gene failed to complement a Saccharomyces cerevisiae mutant indicating that the parasite gene does not belong to the baker’s yeast group, as was previously assumed. Furthermore, Pfdpm1 was unable to complement a mouse mutant deficient in DPM but efficiently complements the Schizosaccharomyces pombe fission yeast mutant, indicating a difference between fission yeast and mammalian DPM genes. Therefore, we reanalyzed the hydrophobicity scales of all known DPMs and consequently reclassify the DPM clade into six major novel subgroups. Furthermore, we show that Pfdpm1 represents a unique enzyme among these subgroups.