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Gene Review

HMG1  -  3-hydroxy-3-methylglutaryl-coenzyme A...

Arabidopsis thaliana

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Disease relevance of HMG1


High impact information on HMG1


Chemical compound and disease context of HMG1


Biological context of HMG1

  • HMG1 and HMG2 consist of four exons and three small introns that interrupt the coding sequence at equivalent positions [8].
  • These findings suggest that HMG1 plays a critical role in triterpene biosynthesis, and that sterols and/or triterpenoids contribute to cell elongation, senescence, and fertility [1].
  • The similarity between the two encoded proteins (HMGR1 and HMGR2) is restricted to the regions corresponding to the membrane and the catalytic domains [8].
  • By using promoter/reporter gene fusions we also demonstrate that this reaction is mediated by cis-acting elements that reside in the Arabidopsis HMG1 promoter and, therefore, is likely to be controlled at the transcriptional level [9].
  • The Arabidopsis HMG1-like proteins contain an HMG domain as a common feature, but outside this conserved DNA-binding motif the amino acid sequences are significantly different indicating that this protein family displays a greater structural variability in plants than in other eukaryotes [2].

Anatomical context of HMG1

  • Our results suggest that the endoplasmic reticulum is the only cell compartment for the targeting of HMGR in Arabidopsis and support the hypothesis that in higher plants the formation of mevalonate occurs solely in the cytosol [8].
  • By using a coupled in vitro transcription-translation assay, we show that both HMGR1 and HMGR2 are cotranslationally inserted into endoplasmic reticulum-derived microsomal membranes [8].
  • Taken together, these data indicate that light-mediated control of the HMG1 gene is mediated by a regulatory circuit that monitors aspects of both spectral quality and fluence and involves either multiple photoreceptors or a single photoreceptor that is differentially sensitive to both blue and red light [9].
  • Taken together, the results reveal that endogenous Arabidopsis HMGR is localized at steady state within ER as expected, but surprisingly also predominantly within spherical, vesicular structures that range from 0.2- to 0.6-microm diameter, located in the cytoplasm and within the central vacuole in differentiated cotyledon cells [10].
  • The results in this paper represent the first evidence that a higher plant HMGR is regulated by direct phosphorylation, at least in a cell-free system [11].

Associations of HMG1 with chemical compounds

  • The sterol levels in hmg1 mutants were lower than in the WT [1].
  • The hmg1 and hmg2 mutants were both more sensitive than the wild type (WT) to lovastatin, an inhibitor of HMGR [1].
  • In contrast, changes in HMG1 mRNA levels were not observed in response to brief light pulses of any spectrum, suggesting that continuous illumination is required for sustained and maximal suppression of HMG coenzyme A reductase expression [9].
  • RNA gel blot analyses using gene-specific probes showed that hmg1 was strongly induced in tuber tissue by wounding, but the wound induction was strongly suppressed by treatment of the tissue with the fungal elicitor arachidonic acid or by inoculation with an incompatible or compatible race of the fungal pathogen Phytophtora infestans [7].
  • Induction of 3-hydroxy-3-methylglutaryl coenzyme A reductase (HMGR) is essential for the biosynthesis of sesquiterpenoid phytoalexins and steroid derivatives in Solanaceous plants following stresses imposed by wounding and pathogen infection [7].

Other interactions of HMG1


Analytical, diagnostic and therapeutic context of HMG1


  1. Loss of function of 3-hydroxy-3-methylglutaryl coenzyme A reductase 1 (HMG1) in Arabidopsis leads to dwarfing, early senescence and male sterility, and reduced sterol levels. Suzuki, M., Kamide, Y., Nagata, N., Seki, H., Ohyama, K., Kato, H., Masuda, K., Sato, S., Kato, T., Tabata, S., Yoshida, S., Muranaka, T. Plant J. (2004) [Pubmed]
  2. Variability in Arabidopsis thaliana chromosomal high-mobility-group-1-like proteins. Stemmer, C., Ritt, C., Igloi, G.L., Grimm, R., Grasser, K.D. Eur. J. Biochem. (1997) [Pubmed]
  3. Overexpression of farnesyl diphosphate synthase in Arabidopsis mitochondria triggers light-dependent lesion formation and alters cytokinin homeostasis. Manzano, D., Busquets, A., Closa, M., Hoyerová, K., Schaller, H., Kamínek, M., Arró, M., Ferrer, A. Plant Mol. Biol. (2006) [Pubmed]
  4. Enhanced seed phytosterol accumulation through expression of a modified HMG-CoA reductase. Hey, S.J., Powers, S.J., Beale, M.H., Hawkins, N.D., Ward, J.L., Halford, N.G. Plant Biotechnol. J. (2006) [Pubmed]
  5. Expression of the Arabidopsis HMG2 gene, encoding 3-hydroxy-3-methylglutaryl coenzyme A reductase, is restricted to meristematic and floral tissues. Enjuto, M., Lumbreras, V., Marín, C., Boronat, A. Plant Cell (1995) [Pubmed]
  6. Targeting and topology in the membrane of plant 3-hydroxy-3-methylglutaryl coenzyme A reductase. Campos, N., Boronat, A. Plant Cell (1995) [Pubmed]
  7. Differential induction and suppression of potato 3-hydroxy-3-methylglutaryl coenzyme A reductase genes in response to Phytophthora infestans and to its elicitor arachidonic acid. Choi, D., Ward, B.L., Bostock, R.M. Plant Cell (1992) [Pubmed]
  8. Arabidopsis thaliana contains two differentially expressed 3-hydroxy-3-methylglutaryl-CoA reductase genes, which encode microsomal forms of the enzyme. Enjuto, M., Balcells, L., Campos, N., Caelles, C., Arró, M., Boronat, A. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  9. Light suppresses 3-Hydroxy-3-methylglutaryl coenzyme A reductase gene expression in Arabidopsis thaliana. Learned, R.M. Plant Physiol. (1996) [Pubmed]
  10. Subcellular localization of Arabidopsis 3-hydroxy-3-methylglutaryl-coenzyme A reductase. Leivar, P., González, V.M., Castel, S., Trelease, R.N., López-Iglesias, C., Arró, M., Boronat, A., Campos, N., Ferrer, A., Fernàndez-Busquets, X. Plant Physiol. (2005) [Pubmed]
  11. Bacterial expression of the catalytic domain of 3-hydroxy-3-methylglutaryl-CoA reductase (isoform HMGR1) from Arabidopsis thaliana, and its inactivation by phosphorylation at Ser577 by Brassica oleracea 3-hydroxy-3-methylglutaryl-CoA reductase kinase. Dale, S., Arró, M., Becerra, B., Morrice, N.G., Boronat, A., Hardie, D.G., Ferrer, A. Eur. J. Biochem. (1995) [Pubmed]
  12. Molecular genetics of plant sterol backbone synthesis. Suzuki, M., Muranaka, T. Lipids (2007) [Pubmed]
  13. Activation of a mitogen-activated protein kinase pathway is involved in disease resistance in tobacco. Yang, K.Y., Liu, Y., Zhang, S. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
  14. Three spinach leaf nitrate reductase-3-hydroxy-3-methylglutaryl-CoA reductase kinases that are required by reversible phosphorylation and/or Ca2+ ions. Douglas, P., Pigaglio, E., Ferrer, A., Halfords, N.G., MacKintosh, C. Biochem. J. (1997) [Pubmed]
  15. Characterization of cDNA and genomic clones encoding 3-hydroxy-3-methylglutaryl-coenzyme A reductase from Hevea brasiliensis. Chye, M.L., Kush, A., Tan, C.T., Chua, N.H. Plant Mol. Biol. (1991) [Pubmed]
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