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Gene Review

HSP12  -  lipid-binding protein HSP12

Saccharomyces cerevisiae S288c

Synonyms: 12 kDa heat shock protein, GLP1, Glucose and lipid-regulated protein, HOR5, YFL014W
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Disease relevance of HSP12

  • Subjecting the yeast to a variety of stresses known to induce HSP12 transcription, including salt, osmotic, ethanol, and heat stress, resulted in a time-dependent increase in GFP fluorescence [1].

High impact information on HSP12


Biological context of HSP12

  • A detailed analysis of the HSP12 promoter region revealed that five repeats of the stress-responsive CCCCT motif (stress-responsive element [STRE]) are essential to confer wild-type induced levels on a reporter gene upon osmostress, heat shock, and entry into stationary phase [4].
  • The [PSI] state did not influence the respective transcript levels nor their regulation, although HSP12 (as a monitor of general stress-responsive) gene expression appeared to differ in the two variant strains [5].
  • The major transcription factors governing (stress-induced) transcriptional activation of HSP12 are Msn2p and Msn4p, binding to the general stress-responsive promoter elements (STREs) [6].
  • Hsp12 accumulates massively in yeast cells exposed to heat shock, osmostress, oxidative stress, and high concentrations of alcohol as well as in early-stationary-phase cells [4].
  • DNA sequence analysis of the cDNA revealed homology with a small heat-shock protein family, HSP12, of Saccharomyces cerevisiae (Sc) [7].

Anatomical context of HSP12


Associations of HSP12 with chemical compounds

  • HSP12 and HSP104 were transcribed 10 h earlier with maltose than with glucose [10].
  • Thus, the HSP26 and the HSP30 promoter can be used for late, phase-specific expression of the desired genes with glucose or maltose as carbon source, and HSP12 with glucose only [10].
  • Another selenium protein identified was a heat-shock protein HSP12 (Mr 11693) in which the only methionine residue was replaced by selenomethionine [11].
  • To analyse the regulatory input of both signal transduction pathways, high-salt-induced HSP12 expression in different genetic backgrounds on glucose-, ethanol- and glycerol-based culture media was examined [12].
  • Despite a previous report that HSP 12 is a heat shock protein, HSP 12 was found to increase in yeast grown at 37 degrees C compared with growth at 30 degrees C. However, increased amounts of HSP 12 were present in yeast after entry into stationary phase; this was enhanced by growth in the osmolytes NaCl and mannitol [13].

Other interactions of HSP12

  • Surprisingly, glucose repression of HSP12 appeared to be independent of Msn2/4p: HSP12 transcription in glycerol-grown cells was unaffected in a deltamsn2deltamsn4 strain [6].
  • Two-dimensional analysis of [3H]-leucine-labelled proteins from salt-shocked cells (0.7 M NaCl) revealed the elevated rate of synthesis of nine proteins, among which were the heat-shock proteins hsp12 and hsp26 [14].
  • Mutation of Ser 102 in the CGFS-motif of Pf Glp1 to cysteine did not generate glutaredoxin activity either [15].
  • Three of the proteins were small molecular weight stress-associated proteins: copper, zinc superoxide-dismutase, ubiquitin, and glucose lipid regulated protein (HSP 12) [16].
  • Molecular models reveal a thioredoxin fold for the putative C-terminal domain of Pf Glp1, Pf Glp2, and Pf Glp3, as well as conserved residues presumably required for glutathione binding [15].

Analytical, diagnostic and therapeutic context of HSP12


  1. A rapid method to determine the stress status of Saccharomyces cerevisiae by monitoring the expression of a Hsp12:green fluorescent protein (GFP) construct under the control of the Hsp12 promoter. Karreman, R.J., Lindsey, G.G. Journal of biomolecular screening : the official journal of the Society for Biomolecular Screening. (2005) [Pubmed]
  2. Roles of the RAM and ANK domains in signaling by the C. elegans GLP-1 receptor. Roehl, H., Bosenberg, M., Blelloch, R., Kimble, J. EMBO J. (1996) [Pubmed]
  3. Displacement of Histones at Promoters of Saccharomyces cerevisiae Heat Shock Genes Is Differentially Associated with Histone H3 Acetylation. Erkina, T.Y., Erkine, A.M. Mol. Cell. Biol. (2006) [Pubmed]
  4. The Saccharomyces cerevisiae HSP12 gene is activated by the high-osmolarity glycerol pathway and negatively regulated by protein kinase A. Varela, J.C., Praekelt, U.M., Meacock, P.A., Planta, R.J., Mager, W.H. Mol. Cell. Biol. (1995) [Pubmed]
  5. Transcriptional regulation of SUP35 and SUP45 in Saccharomyces cerevisiae. Dagkessamanskaya, A., Ter-Avanesyan, M., Mager, W.H. Yeast (1997) [Pubmed]
  6. Very low amounts of glucose cause repression of the stress-responsive gene HSP12 in Saccharomyces cerevisiae. de Groot, E., Bebelman, J.P., Mager, W.H., Planta, R.J. Microbiology (Reading, Engl.) (2000) [Pubmed]
  7. Isolation of an HSP12-homologous gene of Schizosaccharomyces pombe suppressing a temperature-sensitive mutant allele of cdc4. Jang, Y.J., Park, S.K., Yoo, H.S. Gene (1996) [Pubmed]
  8. The LEA-like protein HSP 12 in Saccharomyces cerevisiae has a plasma membrane location and protects membranes against desiccation and ethanol-induced stress. Sales, K., Brandt, W., Rumbak, E., Lindsey, G. Biochim. Biophys. Acta (2000) [Pubmed]
  9. The stress response protein Hsp12p increases the flexibility of the yeast Saccharomyces cerevisiae cell wall. Karreman, R.J., Dague, E., Gaboriaud, F., Quil??s, F., Duval, J.F., Lindsey, G.G. Biochim. Biophys. Acta (2007) [Pubmed]
  10. Phase-specific gene expression in Saccharomyces cerevisiae, using maltose as carbon source under oxygen-limiting conditions. Donalies, U.E., Stahl, U. Curr. Genet. (2001) [Pubmed]
  11. Identification of water-soluble selenium-containing proteins in selenized yeast by size-exclusion-reversed-phase HPLC/ICPMS followed by MALDI-TOF and electrospray Q-TOF mass spectrometry. Encinar, J.R., Ouerdane, L., Buchmann, W., Tortajada, J., Lobinski, R., Szpunar, J. Anal. Chem. (2003) [Pubmed]
  12. High-osmolarity signalling in Saccharomyces cerevisiae is modulated in a carbon-source-dependent fashion. Siderius, M., Rots, E., Mager, W.H. Microbiology (Reading, Engl.) (1997) [Pubmed]
  13. HSP 12 is a LEA-like protein in Saccharomyces cerevisiae. Mtwisha, L., Brandt, W., McCready, S., Lindsey, G.G. Plant Mol. Biol. (1998) [Pubmed]
  14. Osmostress-induced changes in yeast gene expression. Varela, J.C., van Beekvelt, C., Planta, R.J., Mager, W.H. Mol. Microbiol. (1992) [Pubmed]
  15. Plasmodium falciparum glutaredoxin-like proteins. Deponte, M., Becker, K., Rahlfs, S. Biol. Chem. (2005) [Pubmed]
  16. Medicinal yeast extracts. Schlemm, D.J., Crowe, M.J., McNeill, R.B., Stanley, A.E., Keller, S.J. Cell Stress Chaperones (1999) [Pubmed]
  17. Cloning, sequencing and chromosomal assignment of a gene from Saccharomyces cerevisiae which is negatively regulated by glucose and positively by lipids. Stone, R.L., Matarese, V., Magee, B.B., Magee, P.T., Bernlohr, D.A. Gene (1990) [Pubmed]
  18. Development of plant regeneration and transformation protocols for the desiccation-sensitive weeping lovegrass Eragrostis curvula. Ncanana, S., Brandt, W., Lindsey, G., Farrant, J. Plant Cell Rep. (2005) [Pubmed]
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