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Gene Review

JEN1  -  Jen1p

Saccharomyces cerevisiae S288c

Synonyms: Carboxylic acid transporter protein homolog, YKL217W
 
 
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High impact information on JEN1

  • The disruption of JEN1 from Candida albicans impairs the transport of lactate [1].
  • The chimaeric protein Jen1p-GFP is targeted to the plasma membrane via a Sec6-dependent process; upon treatment with glucose, it is endocytosed via END3 and targeted for degradation in the vacuole [2].
  • For example, a strain expressing FLO1 under control of the JEN1 promoter flocculates at a low glucose concentration [3].
  • Activation of the JEN1 promoter requires the Snf1 protein kinase, but multiple regulatory elements most likely combine to provide the linear relationship between JEN1 promoter activity and sugar concentration [3].
  • JEN1 promoter repression is specific to carbon source; heat or cold shock, osmotic stress, DNA damage, and nitrogen starvation do not significantly affect promoter activity [3].
 

Biological context of JEN1

 

Anatomical context of JEN1

 

Associations of JEN1 with chemical compounds

  • JEN1 promoter activity is a linear function of glucose concentration when organisms are grown at a steady-state glucose concentration below 1 g/liter [3].
  • Certain sugars, including glucose, fructose, and mannose, repress the promoter of JEN1, which encodes a lactate-pyruvate transporter, in a dose-dependent manner [3].
  • Cat8p, the activator of gluconeogenic genes in Saccharomyces cerevisiae, regulates carbon source-dependent expression of NADP-dependent cytosolic isocitrate dehydrogenase (Idp2p) and lactate permease (Jen1p) [9].
  • Additional deletion of the JEN1 lactate transporter gene completely blocked uptake of lactate and pyruvate [10].
  • Isogenic strains, deleted in genes encoding enzymes involved in lactic acid metabolism, did not express JEN1, indicating an association of the intracellular metabolism of the acid to the transcription of the permease gene [5].
  • Ubiquitylation and endocytosis of Jen1 are induced within minutes in response to glucose addition [11].
 

Physical interactions of JEN1

  • In this report we demonstrate that, in addition to these regulators, the Hap2/3/4/5 complex interacts specifically with a CAAT-box element in the JEN1 promoter, and acts to derepress JEN1 expression [8].
 

Regulatory relationships of JEN1

  • Expression studies revealed that JEN1 is regulated negatively by the repressors Mig1p and Mig2p, and that Cat8p is needed for full derepression of the gene under non-fermentative growth conditions [9].
 

Other interactions of JEN1

  • The system is based on a Saccharomyces cerevisiae pyk1 mae1 jen1 triple-deletion strain that is auxotrophic for pyruvate and deficient in monocarboxylate uptake [12].
 

Analytical, diagnostic and therapeutic context of JEN1

  • Thus, a JEN1 promoter-reporter system appears to provide a good living cell biosensor for the concentration of certain sugars [3].
  • After 24 h of methanol induction, Northern and Western blotting analyses indicated the expression of JEN1 in the transformants [7].
  • In a DNA microarray analysis, GDR19 highly expressed many more genes, including JEN1, in the presence of glucose compared with the parental strain B29 [13].

References

  1. The disruption of JEN1 from Candida albicans impairs the transport of lactate. Soares-Silva, I., Paiva, S., Kötter, P., Entian, K.D., Casal, M. Mol. Membr. Biol. (2004) [Pubmed]
  2. Utilization of green fluorescent protein as a marker for studying the expression and turnover of the monocarboxylate permease Jen1p of Saccharomyces cerevisiae. Paiva, S., Kruckeberg, A.L., Casal, M. Biochem. J. (2002) [Pubmed]
  3. Saccharomyces cerevisiae JEN1 promoter activity is inversely related to concentration of repressing sugar. Chambers, P., Issaka, A., Palecek, S.P. Appl. Environ. Microbiol. (2004) [Pubmed]
  4. The lactate-proton symport of Saccharomyces cerevisiae is encoded by JEN1. Casal, M., Paiva, S., Andrade, R.P., Gancedo, C., Leão, C. J. Bacteriol. (1999) [Pubmed]
  5. Expression of the lactate permease gene JEN1 from the yeast Saccharomyces cerevisiae. Andrade, R.P., Casal, M. Fungal Genet. Biol. (2001) [Pubmed]
  6. Multiple transcripts regulate glucose-triggered mRNA decay of the lactate transporter JEN1 from Saccharomyces cerevisiae. Andrade, R.P., Kötter, P., Entian, K.D., Casal, M. Biochem. Biophys. Res. Commun. (2005) [Pubmed]
  7. Functional expression of the lactate permease Jen1p of Saccharomyces cerevisiae in Pichia pastoris. Soares-Silva, I., Schuller, D., Andrade, R.P., Baltazar, F., Cássio, F., Casal, M. Biochem. J. (2003) [Pubmed]
  8. Co-ordinate regulation of lactate metabolism genes in yeast: the role of the lactate permease gene JEN1. Lodi, T., Fontanesi, F., Guiard, B. Mol. Genet. Genomics (2002) [Pubmed]
  9. Cat8p, the activator of gluconeogenic genes in Saccharomyces cerevisiae, regulates carbon source-dependent expression of NADP-dependent cytosolic isocitrate dehydrogenase (Idp2p) and lactate permease (Jen1p). Bojunga, N., Entian, K.D. Mol. Gen. Genet. (1999) [Pubmed]
  10. The putative monocarboxylate permeases of the yeast Saccharomyces cerevisiae do not transport monocarboxylic acids across the plasma membrane. Makuc, J., Paiva, S., Schauen, M., Krämer, R., André, B., Casal, M., Leão, C., Boles, E. Yeast (2001) [Pubmed]
  11. Glucose-induced ubiquitylation and endocytosis of the yeast Jen1 transporter: role of lysine 63-linked ubiquitin chains. Paiva, S., Vieira, N., Nondier, I., Haguenauer-Tsapis, R., Casal, M., Urban-Grimal, D. J. Biol. Chem. (2009) [Pubmed]
  12. Co-expression of a mammalian accessory trafficking protein enables functional expression of the rat MCT1 monocarboxylate transporter in Saccharomyces cerevisiae. Makuc, J., Cappellaro, C., Boles, E. FEMS Yeast Res. (2004) [Pubmed]
  13. Analysis of the pyruvate permease gene (JEN1) in glucose derepression yeast (Saccharomyces cerevisiae) Isolated from a 2-deoxyglucose-tolerant mutant, and its application to sake making. Tsuboi, H., Wakisaka, Y., Hirotsune, M., Akao, T., Yamada, O., Akita, O. Biosci. Biotechnol. Biochem. (2003) [Pubmed]
 
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