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Gene Review

PUT4  -  proline permease PUT4

Saccharomyces cerevisiae S288c

Synonyms: O6345, Proline-specific permease, YOR348C
 
 
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High impact information on PUT4

 

Biological context of PUT4

  • A second focus of the review is the nitrogen regulation of the general amino acid permease, Gap1p, and the proline permease, Put4p, by ubiquitin mediated intracellular protein sorting in the secretory and endosomal pathways [6].
  • Put4p downregulation is counteracted by npi1 mutation that affects the cellular ubiquitination function [7].
 

Anatomical context of PUT4

  • 2. GABA transport (Km=3.2+/-0.1 microM and Vmax=0.299+/-0.045 micromol/mg protein min) is probably mediated by a permease similar to Saccharomyces cerevisiae PUT4; this result also indicates that the isolated capillaries are metabolically active [8].
 

Associations of PUT4 with chemical compounds

  • In yeast GABA is also incorporated by the general amino acid permease (GAP1) and the specific proline permease (PUT4) [9].
  • In strains having one class of mutations (per1), ammonia inactivation of the PUT4 and GAP1 permeases did not occur, whereas glutamate and glutamine inactivation did [10].
  • The transport of GABA in Saccharomyces cerevisiae is mediated by three permeases: the general amino acid permease (GAP1), the specific proline permease (PUT4) and a fairly specific GABA permease (UGA4) [11].
  • Low-affinity transport was inhibited by histidine, so put4 mutants were unable to grow on a medium containing high concentrations of proline to which histidine has been added [5].
  • Here we describe mutant Put4 permeases, in which up to nine lysine residues in the cytoplasmic N-terminal domain have been replaced by arginine [7].
 

Other interactions of PUT4

References

  1. A nonconserved Ala401 in the yeast Rsp5 ubiquitin ligase is involved in degradation of Gap1 permease and stress-induced abnormal proteins. Hoshikawa, C., Shichiri, M., Nakamori, S., Takagi, H. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  2. Mutated-gamma-actin restores growth to a yeast amino acid transport defective mutant. Khamessan, A., Naghibalhossaini, F., Vedadi, M., Johnstone, R.M. J. Cell. Physiol. (2001) [Pubmed]
  3. A second nitrogen permease regulator in Saccharomyces cerevisiae. Rousselet, G., Simon, M., Ripoche, P., Buhler, J.M. FEBS Lett. (1995) [Pubmed]
  4. Nucleotide sequence of the Saccharomyces cerevisiae PUT4 proline-permease-encoding gene: similarities between CAN1, HIP1 and PUT4 permeases. Vandenbol, M., Jauniaux, J.C., Grenson, M. Gene (1989) [Pubmed]
  5. Proline transport in Saccharomyces cerevisiae. Lasko, P.F., Brandriss, M.C. J. Bacteriol. (1981) [Pubmed]
  6. Nitrogen regulation in Saccharomyces cerevisiae. Magasanik, B., Kaiser, C.A. Gene (2002) [Pubmed]
  7. Engineering of yeast Put4 permease and its application to lager yeast for efficient proline assimilation. Omura, F., Fujita, A., Miyajima, K., Fukui, N. Biosci. Biotechnol. Biochem. (2005) [Pubmed]
  8. Delta-aminolevulinic acid transport through blood-brain barrier. García, S.C., Moretti, M.B., Garay, M.V., Batlle, A. Gen. Pharmacol. (1998) [Pubmed]
  9. Carbon and nitrogen sources regulate delta-aminolevulinic acid and gamma-aminobutyric acid transport in Saccharomyces cerevisiae. Correa García, S., Bermúdez Moretti, M., Ramos, E., Batlle, A. Int. J. Biochem. Cell Biol. (1997) [Pubmed]
  10. Ammonia regulation of amino acid permeases in Saccharomyces cerevisiae. Courchesne, W.E., Magasanik, B. Mol. Cell. Biol. (1983) [Pubmed]
  11. delta-Aminolevulinic acid uptake is mediated by the gamma-aminobutyric acid-specific permease UGA4. Bermúdez Moretti, M., Correa García, S., Ramos, E., Batlle, A. Cell. Mol. Biol. (Noisy-le-grand) (1996) [Pubmed]
  12. UGA4 gene expression in Saccharomyces cerevisiae depends on cell growth conditions. Bermúdez Moretti, M., Correa García, S., Batlle, A. Cell. Mol. Biol. (Noisy-le-grand) (1998) [Pubmed]
  13. Construction of phosphatidylethanolamine-less strain of Saccharomyces cerevisiae. Effect on amino acid transport. Robl, I., Grassl, R., Tanner, W., Opekarová, M. Yeast (2001) [Pubmed]
 
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