A differentiation-dependend polyisoprenol kinase in Dictyostelium discoideum

Abstract

Crude membrane fractions of Dictyostelium discoideum show the capacity to synthesize (1--3H)dolicholphosphate from (1--3H)dolichol. Formation of dolicholphosphate increased continuously over the first 15 min. The reaction rate was nearly linear with respect to the dolichol content up to 150 microM. The phosphate donor for the reaction is CTP. The optimum concentration of CTP is about 0,75 mM. The reaction is dependent on divalent metal ions, magnesium being more effective than calcium or manganese. The activity of the polyisoprenol kinase depends on the course of the early development. Maximum enzyme activities are present 4--6 h after the induction of the differentiation.

Arabidopsis DOK1 encodes a functional dolichol kinase involved in reproduction

“…We searched for cytidylyltransferase motif-containing genes in Arabidopsis because DOK is predicted to be a CTP-dependent cytidylyltransferase (Keller et al, 1982;Rossler et al, 1982;Rip and Carroll, 1988;Szkopinska et al, 1988;Rymerson et al, 1992). Arabidopsis has at least 13 genes annotated to encode cytidylyltransferase motif-containing proteins (Table 1), most of which are involved in phospholipid biosynthesis (Kopka et al, 1997;Inatsugi et al, 2002;Mizoi et al, 2006;Haselier et al, 2010;Zhou et al, 2013).…”

“…The second pathway first gives rise to dolichol as the end product of de novo synthesis, and then a dolichol kinase (DOK) phosphorylates dolichol to synthesize Dol‐P (Rossignol et al ., ). DOK activity has been previously described in rat liver microsomes (Keller et al ., ), Dictyostelium discoideum (slime mold) (Rossler et al ., ), Glycine max (soybean) embryos (Rip and Carroll, ), Saccharomyces cerevisiae (budding yeast) (Szkopinska et al ., ) and etiolated Secale cereale (rye) seedlings (Rymerson et al ., ). Because these activities are cytidine triphosphate (CTP)‐dependent, DOK may be encoded by a cytidylyltransferase family gene.…”

Expression and characterization of a human cDNA that complements the temperature-sensitive defect in dolichol kinase activity in the yeast sec59-1 mutant: the enzymatic phosphorylation of dolichol and diacylglycerol are catalyzed by separate CTP-mediated kinase activities in Saccharomyces cerevisiae

“…However, it has not been previously determined if the phosphorylation of diacylglycerol (DAG) and dolichol are catalyzed by a single or separate CTP-mediated kinases in S. cerevisiae. Moreover, developmental changes in DK activity have been reported for sea urchin embryos (Rossignol et al, 1981), estrogen-treated chick oviducts (Burton et al, 1981); Dictyostelium discoideum (Rossler et al, 1982), and pig (Scher et al, 1985) and rat brain (Volpe et al, 1987;Bhat et al, 1991). However, the molecular tools have not been available to assess whether these changes in activity were due to different levels of expression or modification of the CTP-mediated enzyme.…”

Human Dolichol Kinase, a Polytopic Endoplasmic Reticulum Membrane Protein with a Cytoplasmically Oriented CTP-binding Site

“…The enzymatic transfer of phosphoryl groups from CTP to dolichol catalyzed by microsomal fractions from mammalian cells was first detected more than 20 years ago (3,4). Developmental changes in dolichol kinase (DK) activity corresponding to an increased capacity for protein N-glycosylation have been reported for sea urchin embryos (5), estrogen-treated chick oviducts (6), Dictyostelium discoideum (7), and pig (8) and rat brain (9,10). If the enzymatic reduction of the ␣-isoprene unit in dolichol occurs at the free polyprenol level as proposed by Sagami et al (11), DK would catalyze the final step in the de novo pathway for Dol-P biosynthesis (1).…”