Mevinolin-resistant mutations identify a promoter and the gene for a eukaryote-like 3-hydroxy-3-methylglutaryl-coenzyme A reductase in the archaebacterium Haloferax volcanii.

@article{Lam1992MevinolinresistantMI,
  title={Mevinolin-resistant mutations identify a promoter and the gene for a eukaryote-like 3-hydroxy-3-methylglutaryl-coenzyme A reductase in the archaebacterium Haloferax volcanii.},
  author={Wan L. Lam and W. Ford Doolittle},
  journal={The Journal of biological chemistry},
  year={1992},
  volume={267 9},
  pages={
          5829-34
        }
}
  • W. Lam, W. Doolittle
  • Published 25 March 1992
  • Medicine, Biology
  • The Journal of biological chemistry
Both eukaryotes and archaebacteria use 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase to synthesize mevalonate, which eukaryotes employ in the production of sterols and archaebacteria need for the isoprenoid side chains of their unique and characteristic lipids. The drug mevinolin inhibits HMG-CoA reductase in eukaryotes and in the halophilic archaebacteria, and we have used a spontaneous mutation to mevinolin resistance in the construction of a selectable shuttle vector for… Expand
3-hydroxy-3-methylglutaryl coenzyme A reductase of Sulfolobus solfataricus: DNA sequence, phylogeny, expression in Escherichia coli of the hmgA gene, and purification and kinetic characterization of the gene product
TLDR
The gene (hmgA) for 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase from the thermophilic archaeon Sulfolobus solfataricus P2 was cloned and sequenced and suggested that the two archaeal genes are distant homologs of eukaryotic genes. Expand
Cloning of the gene encoding 3-hydroxy-3-methylglutaryl coenzyme A reductase from terpenoid antibiotic-producing Streptomyces strains
TLDR
A mutant lacking 3-hydroxy-3-methylglutaryl CoA (HMG-CoA) reductase activity is isolated from a terpenoid antibiotic producer, Streptomyces griseolosporeus MF730-N6, which uses both the mevalonate and nonmeValonate pathways for the formation of isopentenyl diphosphate by screening terpentecin non-producing mutants. Expand
3-Hydroxy-3-methylglutaryl-coenzyme A reductase from Haloferax volcanii: purification, characterization, and expression in Escherichia coli
TLDR
The characterization of an HMG-CoA reductase from the third domain, the archaea is reported, suggesting a similar catalytic mechanism to that of homogeneous hamster or P. mevalonii. Expand
A new simvastatin (mevinolin)-resistance marker from Haloarcula hispanica and a new Haloferax volcanii strain cured of plasmid pHV2.
The mevinolin-resistance determinant, hmg, encodes the enzyme 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase and is a commonly used selectable marker in halobacterial genetics. PlasmidsExpand
Molecular, functional and evolutionary characterization of the gene encoding HMG‐CoA reductase in the fission yeast, Schizosaccharomyces pombe
TLDR
Gene disruption analysis showed that hmg1+ was an essential gene, and provided evidence that, unlike Saccharomyces cerevisiae, S. pombe contained only a single functional HMG‐CoA reductase gene. Expand
Disruption of a Sugar Transporter Gene Cluster in a Hyperthermophilic Archaeon Using a Host-Marker System Based on Antibiotic Resistance
ABSTRACT We have developed a gene disruption system in the hyperthermophilic archaeon Thermococcus kodakaraensis using the antibiotic simvastatin and a fusion gene designed to overexpress theExpand
3-Hydroxy-3-methylglutaryl-CoA reductase gene of Gibberella fujikuroi: isolation and characterization
TLDR
Sequence analysis revealed a high degree of similarity between the deduced amino-acid sequences in the C-terminal catalytic domains of all known HMG-CoA reductases, but the highest degree was found between the sequences of both analysed ascomycetes. Expand
Sequence comparison of a segment of the gene for 3-hydroxy-3-methylglutaryl-coenzyme A reductase in zygomycetes.
TLDR
Comparisons of sequences of a segment of the 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase gene, isolated from eleven different strains belonging to four species of the fungal order Mucorales, show sequence similarity of around 80% at the protein sequence level, whereas sequences of the same type from different species show similarity ranging between 91-96%. Expand
Partial silencing of a hydroxy-methylglutaryl-CoA reductase-encoding gene in Trichoderma harzianum CECT 2413 results in a lower level of resistance to lovastatin and lower antifungal activity.
TLDR
The cloning and characterization of the Trichoderma harzianum hmgR gene encoding a hydroxymethylglutaryl CoA reductase (HMGR), a key enzyme in the biosynthesis of terpene compounds, are described and a reduction in their antifungal activity against the plant-pathogen fungi Rhizoctonia solani and Fusarium oxysporum is shown. Expand
Molecular cloning, developmental pattern and tissue expression of 3-hydroxy-3-methylglutaryl coenzyme A reductase of the cockroach Blattella germanica.
TLDR
Northern-blot analysis of RNA samples from different adult female tissues shows high HMG-CoA reductase mRNA levels in the ovary and lower levels in brain and muscle, and analysis of B. germanica H MG- coenzyme A reduct enzyme mRNA levels reveals a 3.6-kb transcript, that is overexpressed in 4-day-old embryos. Expand
...
1
2
3
4
5
...