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Gene Review

HMG1  -  hydroxymethylglutaryl-CoA reductase...

Saccharomyces cerevisiae S288c

Synonyms: 3-hydroxy-3-methylglutaryl-coenzyme A reductase 1, HMG-CoA reductase 1, YML075C
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Disease relevance of HMG1

  • A C-terminal-truncated fragment of the U. maydis HMG-CoA reductase gene was shown to be expressed in Escherichia coli in a catalytically active form [1].
  • HMG-CoA reductase inhibitors are very efficient in long-term control of atherogenesis acting by different mechanisms not fully established [2].

High impact information on HMG1


Biological context of HMG1


Anatomical context of HMG1


Associations of HMG1 with chemical compounds


Other interactions of HMG1

  • Cells containing mutant alleles of both HMG1 and HMG2 are unable to undergo spore germination and vegetative growth [15].
  • The predicted SIN1/SPT2 protein has a distinctive amino acid composition (45% charged residues, 25% basic and 20% acidic) and has similarity to the mammalian HMG1 protein, a nonhistone component of chromatin [18].
  • Taken together, the data indicate that HMO1 is likely to be the homolog of HMG1/2 in higher cells and that it plays an important role in genome maintenance [19].
  • The Saccharomyces cerevisiae ACP2 gene encodes an essential HMG1-like protein [20].
  • SHM1: a multicopy suppressor of a temperature-sensitive null mutation in the HMG1-like abf2 gene [21].

Analytical, diagnostic and therapeutic context of HMG1


  1. Isolation of an Ustilago maydis gene encoding 3-hydroxy-3-methylglutaryl-coenzyme A reductase and expression of a C-terminal-truncated form in Escherichia coli. Croxen, R., Goosey, M.W., Keon, J.P., Hargreaves, J.A. Microbiology (Reading, Engl.) (1994) [Pubmed]
  2. Effects of pravastatin on the in vitro phagocytic function and hydrogen peroxide production by monocytes of healthy individuals. Muniz-Junqueira, M.I., Karnib, S.R., de Paula-Coelho, V.N., Junqueira, L.F. Int. Immunopharmacol. (2006) [Pubmed]
  3. Crystal structure of double-stranded DNA containing the major adduct of the anticancer drug cisplatin. Takahara, P.M., Rosenzweig, A.C., Frederick, C.A., Lippard, S.J. Nature (1995) [Pubmed]
  4. Regulation of HMG-CoA reductase degradation requires the P-type ATPase Cod1p/Spf1p. Cronin, S.R., Khoury, A., Ferry, D.K., Hampton, R.Y. J. Cell Biol. (2000) [Pubmed]
  5. A 'distributed degron' allows regulated entry into the ER degradation pathway. Gardner, R.G., Hampton, R.Y. EMBO J. (1999) [Pubmed]
  6. Degradation of HMG-CoA reductase-induced membranes in the fission yeast, Schizosaccharomyces pombe. Lum, P.Y., Wright, R. J. Cell Biol. (1995) [Pubmed]
  7. The Saccharomyces cerevisiae DNA polymerase alpha catalytic subunit interacts with Cdc68/Spt16 and with Pob3, a protein similar to an HMG1-like protein. Wittmeyer, J., Formosa, T. Mol. Cell. Biol. (1997) [Pubmed]
  8. Identifying mutations in duplicated functions in Saccharomyces cerevisiae: recessive mutations in HMG-CoA reductase genes. Basson, M.E., Moore, R.L., O'Rear, J., Rine, J. Genetics (1987) [Pubmed]
  9. A hap1 mutation in a laboratory strain of Saccharomyces cerevisiae results in decreased expression of ergosterol-related genes and cellular ergosterol content compared to sake yeast. Tamura, K., Gu, Y., Wang, Q., Yamada, T., Ito, K., Shimoi, H. J. Biosci. Bioeng. (2004) [Pubmed]
  10. Recruitment of mRNA cleavage/polyadenylation machinery by the yeast chromatin protein Sin1p/Spt2p. Hershkovits, G., Bangio, H., Cohen, R., Katcoff, D.J. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  11. Increased amounts of HMG-CoA reductase induce "karmellae": a proliferation of stacked membrane pairs surrounding the yeast nucleus. Wright, R., Basson, M., D'Ari, L., Rine, J. J. Cell Biol. (1988) [Pubmed]
  12. Identification of the sequences in HMG-CoA reductase required for karmellae assembly. Parrish, M.L., Sengstag, C., Rine, J.D., Wright, R.L. Mol. Biol. Cell (1995) [Pubmed]
  13. Amino-terminal sequence of a Saccharomyces cerevisiae nuclear protein, NHP6, shows significant identity to bovine HMG1. Kolodrubetz, D., Haggren, W., Burgum, A. FEBS Lett. (1988) [Pubmed]
  14. Recombinant HMG1 protein produced in Pichia pastoris: a nonviral gene delivery agent. Mistry, A.R., Falciola, L., Monaco, L., Tagliabue, R., Acerbis, G., Knight, A., Harbottle, R.P., Soria, M., Bianchi, M.E., Coutelle, C., Hart, S.L. BioTechniques (1997) [Pubmed]
  15. Saccharomyces cerevisiae contains two functional genes encoding 3-hydroxy-3-methylglutaryl-coenzyme A reductase. Basson, M.E., Thorsness, M., Rine, J. Proc. Natl. Acad. Sci. U.S.A. (1986) [Pubmed]
  16. Regulation of partitioned sterol biosynthesis in Saccharomyces cerevisiae. Casey, W.M., Keesler, G.A., Parks, L.W. J. Bacteriol. (1992) [Pubmed]
  17. ERG10 from Saccharomyces cerevisiae encodes acetoacetyl-CoA thiolase. Hiser, L., Basson, M.E., Rine, J. J. Biol. Chem. (1994) [Pubmed]
  18. A negative regulator of HO transcription, SIN1 (SPT2), is a nonspecific DNA-binding protein related to HMG1. Kruger, W., Herskowitz, I. Mol. Cell. Biol. (1991) [Pubmed]
  19. Characterization of a high mobility group 1/2 homolog in yeast. Lu, J., Kobayashi, R., Brill, S.J. J. Biol. Chem. (1996) [Pubmed]
  20. The Saccharomyces cerevisiae ACP2 gene encodes an essential HMG1-like protein. Haggren, W., Kolodrubetz, D. Mol. Cell. Biol. (1988) [Pubmed]
  21. SHM1: a multicopy suppressor of a temperature-sensitive null mutation in the HMG1-like abf2 gene. Kao, L.R., Megraw, T.L., Chae, C.B. Yeast (1996) [Pubmed]
  22. Transmission electron microscopy and immunocytochemical studies of yeast: analysis of HMG-CoA reductase overproduction by electron microscopy. Wright, R., Rine, J. Methods Cell Biol. (1989) [Pubmed]
  23. Isolation and structural characterization of a cDNA encoding Arabidopsis thaliana 3-hydroxy-3-methylglutaryl coenzyme A reductase. Caelles, C., Ferrer, A., Balcells, L., Hegardt, F.G., Boronat, A. Plant Mol. Biol. (1989) [Pubmed]
  24. 3-Hydroxy-3-methylglutaryl coenzyme A reductase in the sea urchin embryo is developmentally regulated. Woodward, H.D., Allen, J.M., Lennarz, W.J. J. Biol. Chem. (1988) [Pubmed]
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