Molecular Cloning and Expression of the cDNAs Encoding Human and Yeast Mevalonate Pyrophosphate Decarboxylase

Toth, Matthew J.; Huwyler, Leslie

doi:10.1074/jbc.271.14.7895

Cited by 53 publications

(38 citation statements)

References 14 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Molecular Biology of the Cellof significant sequence similarity to the budding yeast genes CYT2 (cytochrome-c1 heme lyase) (Zollner et al, 1992) and MVD1 (mevalonate diphosphate decarboxylase) (Toth and Huwyler, 1996).…”

Section: Rr West Et Almentioning

confidence: 99%

“…This analysis identified two neighboring genes: cyt2 ϩ , which overlaps with cut11 ϩ on the opposite DNA strand, and mvd1 ϩ , which lies downstream on the same strand. These genes were named on the basis of significant sequence similarity to the budding yeast genes CYT2 (cytochrome-c1 heme lyase) (Zollner et al, 1992) and MVD1 (mevalonate diphosphate decarboxylase) (Toth and Huwyler, 1996). …”

mentioning

confidence: 99%

See 1 more Smart Citation

cut11⁺: A Gene Required for Cell Cycle-dependent Spindle Pole Body Anchoring in the Nuclear Envelope and Bipolar Spindle Formation inSchizosaccharomyces pombe

West

Vaisberg

Ding

et al. 1998

MBoC

159

197

View full text Add to dashboard Cite

The "cut" mutants of Schizosaccharomyces pombe are defective in spindle formation and/or chromosome segregation, but they proceed through the cell cycle, resulting in lethality. Analysis of temperature-sensitive alleles of cut11 ϩ suggests that this gene is required for the formation of a functional bipolar spindle. Defective spindle structure was revealed with fluorescent probes for tubulin and DNA. Three-dimensional reconstruction of mutant spindles by serial sectioning and electron microscopy showed that the spindle pole bodies (SPBs) either failed to complete normal duplication or were free floating in the nucleoplasm. Localization of Cut11p tagged with the green fluorescent protein showed punctate nuclear envelope staining throughout the cell cycle and SPBs staining from early prophase to mid anaphase. This SPB localization correlates with the time in the cell cycle when SPBs are inserted into the nuclear envelope. Immunoelectron microscopy confirmed the localization of Cut11p to mitotic SPBs and nuclear pore complexes. Cloning and sequencing showed that cut11 ϩ encodes a novel protein with seven putative membrane-spanning domains and homology to the Saccharomyces cerevisiae gene NDC1. These data suggest that Cut11p associates with nuclear pore complexes and mitotic SPBs as an anchor in the nuclear envelope; this role is essential for mitosis. INTRODUCTIONAccurate chromosome segregation requires proper assembly and function of a mitotic spindle. The spindle is constructed from microtubules (MT) 1 whose polymerization is nucleated by the centrosome (reviewed in Kellogg et al., 1994), which is known in fungi as the spindle pole body (SPB) (reviewed in Snyder, 1994). Although these two organelles are structurally distinct, genetic and biochemical approaches have identified several common components of centrosomes and SPBs, including ␥-tubulin (reviewed in Kellogg et al., 1994), CDC31/centrin (reviewed in Schiebel and Bornes, 1995), and p34 cdc2 (Bailly et al., 1989; Raibowol et al., 1989). Thus, analyses of SPBs have been informative about centrosomes in general.Recent work has demonstrated that the SPB of Schizosaccharomyces pombe is a dynamic organelle, undergoing significant changes in morphology and cellular localization as cells progress through their growth and division cycle (Ding et al., 1997). The nature of these changes distinguishes the fission yeast centrosome from that of other organisms. For example, the SPBs of the budding yeast Saccharomyces cer- evisiae duplicate in G 1 and remain in the nuclear envelope through the entire cell cycle (Byers, 1981;. The fission yeast SPB, on the other hand, resides in the cytoplasm through most of interphase, where it duplicates during late G 2 . As the cell enters mitosis, the nuclear envelope invaginates beneath the SPB and forms an opening, or fenestra, into which the duplicated SPB settles. Each part of the double SPB initiates intranuclear MTs; then the two parts separate to lie in distinct fenestrae, bound to the polar ends of the spindle MTs. As anaphas...

show abstract

Section: Rr West Et Almentioning

confidence: 99%

mentioning

confidence: 99%

cut11⁺: A Gene Required for Cell Cycle-dependent Spindle Pole Body Anchoring in the Nuclear Envelope and Bipolar Spindle Formation inSchizosaccharomyces pombe

West

Vaisberg

Ding

et al. 1998

MBoC

159

197

View full text Add to dashboard Cite

show abstract

“…The MVD activity has been quantified in animals [19], plants [20], and yeast. [21] MVD can be used as a potential target of several diseases, such as cancer and restenosis [22].…”

Section: Introductionmentioning

confidence: 99%

Molecular cloning and expression analysis of mevalonate pyrophosphate decarboxylase inAntrodia cinnamomea

Lin

Shao

et al. 2016

MATEC Web of Conferences

View full text Add to dashboard Cite

Abstract. Mevalonate pyrophosphate decarboxylase (MVD) plays important roles in triterpenoid biosynthesis via the mevalonate pathway. A novel MVD gene was isolated and identified in Antrodia cinnamomea (Ac-mvd). The fulllength cDNA contained an open reading frame with a length of 1,209 bp and encoded a 402-amino acid polypeptide with a molecular mass of 43.3 kDa and a theoretical pI of 8.23. As incubation time was prolonged for 28 days, the triterpenoid content in the mycelium gradually increased and reached 39.192 ± 2.025 mg/g; the triterpenoid content of the fruiting body grew in the hay of Cinnamomum kanehirae (ACFB-CK), was 49.391 ± 2.675 mg/g, which was significantly different from other samples (P < 0.05). qRT-PCR revealed that the highest expression levels of Ac-mvd in the mycelium of Antrodia cinnamomea were detected on the 7th day. The expression levels gradually decreased as culture time was extended from 14 days to 42 days.

show abstract

“…Toth and Huwyler reported cDNA sequences of MPD from human liver and yeast. 10) The recombinant human enzyme is a homodimer of 43-kDa subunits with 400 amino acids. We recently established a procedure for the purification of MPD from the liver of rats fed a diet containing 5% cholestyramine and 0.1% pravastatin (CP diet) using chromatography and polyclonal antiserum raised against rat MPD.…”

mentioning

confidence: 99%

Purification and Characterization of Mouse Mevalonate Pyrophosphate Decarboxylase.

Michihara

Akasaki

Yamori

et al. 2002

Biological & Pharmaceutical Bulletin

View full text Add to dashboard Cite

One of the first steps in the biosynthesis of cholesterol from acetic acid is catalyzed by mevalonate pyrophosphate decarboxylase (MPD). This decarboxylase catalyzes a bimolecular reaction between mevalonate 5-pyrophosphate (MVAPP) and ATP to form isopentenyl pyrophosphate, inorganic phosphate, adenosine-5Ј-diphosphate (ADP), and CO 2 .MPD has been purifed from various sources including yeast, 1,2) latex of Hevea brasiliensis, 3) pig liver, 4,5) rat liver, [6][7][8] and chicken liver. 9) Its properties in rat and chicken have been examined in detail. Toth and Huwyler reported cDNA sequences of MPD from human liver and yeast.10) The recombinant human enzyme is a homodimer of 43-kDa subunits with 400 amino acids. We recently established a procedure for the purification of MPD from the liver of rats fed a diet containing 5% cholestyramine and 0.1% pravastatin (CP diet) using chromatography and polyclonal antiserum raised against rat MPD. 8)Epidemiological studies have indicated a negative association between the serum cholesterol level and the incidence of cerebral hemorrhage in humans.11) Spontaneously hypertensive rat stroke-prone (SHRSP) is a widely used animal model for hypertension and stroke.12) Iritani et al. reported that the serum cholesterol level in SHRSP was low when compared with that in normotensive age-matched Wistar Kyoto rats (WKY). 13) We previously reported that the low serum cholesterol level in SHRSP as compared with WKY may be attributable to the reduced activity of MPD and not 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase. 14) Moreover, we found that the decline in activity was caused by a reduction in the amount of enzyme in SHRSP.15) As described above, it is important to understand the mechanism of the decrease in MPD. We are also very interested in whether MPDknockout or MPD-reduced mice experience cerebral hemorrhage. However, information on MPD in normal mice is relatively scarce.In this paper, we describe a simple procedure for the purification of MPD from mouse liver, the properties of MPD, and a comparison of this MPD with counterparts from other animals. MATERIALS AND METHODSMaterials Pharmalyte 3-10 for isoelectric focusing and Western blotting detection kits were purchased from Amersham Pharmacia Biotech. Affigel 10 and 15 were obtained from Bio-Rad. RS-[ 3 H] mevalonolactone was purchased from Du Pont-New England Nuclear. Albumin from rat fraction V was purchased from Wako Chemicals. ddy Mice (8 weeks of age) were obtained from Shimizu Experimental Animals. All other chemicals were of reagent grade and purchased from commercial sources.Radioactive Assay The activities of the crude extract as well as the purified enzyme were measured according to the method of Sawamura et al.14) Unless otherwise indicated, the reaction mixture consisted of 100 mM Tris-HCl (pH 7.2), 5 mM ATP, 5 mM MgCl 2 , 10 mM NaF, Purification of MPD in RatsPurification of rat liver MPD was carried out as described by Michihara et al. 8)Preparation of an Affinity Column with Anti-rat MPD Antibody We...

show abstract

Molecular Cloning and Expression of the cDNAs Encoding Human and Yeast Mevalonate Pyrophosphate Decarboxylase

Cited by 53 publications

References 14 publications

cut11⁺: A Gene Required for Cell Cycle-dependent Spindle Pole Body Anchoring in the Nuclear Envelope and Bipolar Spindle Formation inSchizosaccharomyces pombe

cut11⁺: A Gene Required for Cell Cycle-dependent Spindle Pole Body Anchoring in the Nuclear Envelope and Bipolar Spindle Formation inSchizosaccharomyces pombe

Molecular cloning and expression analysis of mevalonate pyrophosphate decarboxylase inAntrodia cinnamomea

Purification and Characterization of Mouse Mevalonate Pyrophosphate Decarboxylase.

Contact Info

Product

Resources

About

Molecular Cloning and Expression of the cDNAs Encoding Human and Yeast Mevalonate Pyrophosphate Decarboxylase

Cited by 53 publications

References 14 publications

cut11+: A Gene Required for Cell Cycle-dependent Spindle Pole Body Anchoring in the Nuclear Envelope and Bipolar Spindle Formation inSchizosaccharomyces pombe

cut11+: A Gene Required for Cell Cycle-dependent Spindle Pole Body Anchoring in the Nuclear Envelope and Bipolar Spindle Formation inSchizosaccharomyces pombe

Molecular cloning and expression analysis of mevalonate pyrophosphate decarboxylase inAntrodia cinnamomea

Purification and Characterization of Mouse Mevalonate Pyrophosphate Decarboxylase.

Contact Info

Product

Resources

About

cut11⁺: A Gene Required for Cell Cycle-dependent Spindle Pole Body Anchoring in the Nuclear Envelope and Bipolar Spindle Formation inSchizosaccharomyces pombe

cut11⁺: A Gene Required for Cell Cycle-dependent Spindle Pole Body Anchoring in the Nuclear Envelope and Bipolar Spindle Formation inSchizosaccharomyces pombe