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Gene Review

ENO2  -  phosphopyruvate hydratase ENO2

Saccharomyces cerevisiae S288c

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High impact information on ENO2

  • HOG1 was also required for citric acid-induced up-regulation of Ssa1p and Eno2p [1].
  • A complex regulatory element from the yeast gene ENO2 modulates GCR1-dependent transcriptional activation [2].
  • UAS elements which bound the RAP1 protein or the ABFI protein modulated glucose-dependent induction of ENO1 and ENO2 expression [3].
  • The ABFI-binding site in ENO2 overlapped sequences required for UAS2 activity in wild-type strains and for repression of ENO2 expression in strains carrying a null mutation in the positive regulatory gene GCR1 [3].
  • A small deletion mutation within one of two upstream activation sites (UAS elements) in the 5'-flanking region of ENO2 permitted wild-type levels of ENO2 gene expression in a strain carrying the gcr1 null mutation [4].

Biological context of ENO2


Anatomical context of ENO2

  • Either deletion of the non-essential ENO1 gene or diminished expression of the essential ENO2 gene causes vacuole fragmentation in vivo, reflecting reduced fusion [5].

Associations of ENO2 with chemical compounds

  • The effect of the ENO2 upstream activation sequence on expression of yeast LEU2 was studied [8].
  • The upstream activation sequence from ENO2, one of two genes coding for yeast enolase, was inserted into the upstream 405 HpaI site of LEU2, which codes for beta-isopropylmalate dehydrogenase (E.C., utilizing shuttle plasmid YEp13 [8].

Regulatory relationships of ENO2

  • In contrast, ENO2 expression is induced more than 20-fold in cells grown on glucose as the carbon source. cis-Acting regulatory sequences were mapped within the 5'-flanking region of the constitutively expressed yeast enolase gene ENO1 [7].

Other interactions of ENO2

  • Here we purify this activity and identify it as enolase (Eno1p and Eno2p) [5].
  • During the transition to non-growing states (-N and -NC states), the levels of Hxk2p, Tdh3p and Eno2p were further reduced [9].


  1. Evidence of a new role for the high-osmolarity glycerol mitogen-activated protein kinase pathway in yeast: regulating adaptation to citric acid stress. Lawrence, C.L., Botting, C.H., Antrobus, R., Coote, P.J. Mol. Cell. Biol. (2004) [Pubmed]
  2. A complex regulatory element from the yeast gene ENO2 modulates GCR1-dependent transcriptional activation. Willett, C.E., Gelfman, C.M., Holland, M.J. Mol. Cell. Biol. (1993) [Pubmed]
  3. Multiple factors bind the upstream activation sites of the yeast enolase genes ENO1 and ENO2: ABFI protein, like repressor activator protein RAP1, binds cis-acting sequences which modulate repression or activation of transcription. Brindle, P.K., Holland, J.P., Willett, C.E., Innis, M.A., Holland, M.J. Mol. Cell. Biol. (1990) [Pubmed]
  4. Sequences within an upstream activation site in the yeast enolase gene ENO2 modulate repression of ENO2 expression in strains carrying a null mutation in the positive regulatory gene GCR1. Holland, J.P., Brindle, P.K., Holland, M.J. Mol. Cell. Biol. (1990) [Pubmed]
  5. Enolase activates homotypic vacuole fusion and protein transport to the vacuole in yeast. Decker, B.L., Wickner, W.T. J. Biol. Chem. (2006) [Pubmed]
  6. Identification of a regulatory region that mediates glucose-dependent induction of the Saccharomyces cerevisiae enolase gene ENO2. Cohen, R., Holland, J.P., Yokoi, T., Holland, M.J. Mol. Cell. Biol. (1986) [Pubmed]
  7. Transcription of the constitutively expressed yeast enolase gene ENO1 is mediated by positive and negative cis-acting regulatory sequences. Cohen, R., Yokoi, T., Holland, J.P., Pepper, A.E., Holland, M.J. Mol. Cell. Biol. (1987) [Pubmed]
  8. Effect on yeast LEU2 expression of upstream activation sequence from yeast ENO2 gene coding for enolase. Wang, E.D., Holland, M. Chin. J. Biotechnol. (1989) [Pubmed]
  9. Fermentative capacity after cold storage of baker's yeast is dependent on the initial physiological state but not correlated to the levels of glycolytic enzymes. Nilsson, A., Norbeck, J., Oelz, R., Blomberg, A., Gustafsson, L. Int. J. Food Microbiol. (2001) [Pubmed]
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