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Gene Review

PUT3  -  Put3p

Saccharomyces cerevisiae S288c

Synonyms: Proline utilization trans-activator, YKL015W
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Disease relevance of PUT3


High impact information on PUT3

  • Modulation of transcription factor function by an amino acid: activation of Put3p by proline [2].
  • The activation of Put3p requires no additional yeast proteins and can occur in the presence of certain proline analogues: an unmodified pyrrolidine ring is able to activate Put3p as efficiently as proline itself [2].
  • Cloning of the gene for this endonuclease was achieved by chromosome walking from the nearby PUT3 locus [3].
  • Comparisons with the DNA complexes of the related GAL4, PPR1 and PUT3 proteins illustrate how a conserved protein domain can be reoriented to recognize DNA half sites of different polarities and how homodimeric proteins adopt dramatically asymmetric structures to recognize cognate DNA targets [4].
  • Furthermore, we have characterized the dynamics of PUT3 to find that the zinc cluster and dimerization domains have very diverse dynamics in solution [5].

Biological context of PUT3

  • Wild-type levels of complex formation were observed in an extract of a strain carrying an allele of PUT3 that resulted in a constitutive (Put+) phenotype [6].
  • In vitro complex formation was observed in crude extracts of yeast strains carrying either a single genomic copy of the PUT3 gene or the cloned PUT3 gene on a 2 microns plasmid, and the binding was dosage dependent [6].
  • One activator-defective and seven activator-constitutive PUT3 alleles have been retrieved from the genome and sequenced to determine the nucleotide changes responsible for the altered function of the protein [7].
  • The sequence of the wild-type PUT3 gene revealed the presence of one large open reading frame capable of encoding a 979-amino-acid protein [7].
  • The PUT3 gene maps on chromosome XI, about 5.7 cM from the centromere [8].

Associations of PUT3 with chemical compounds


Physical interactions of PUT3

  • We conclude that the PUT3 product is either a DNA-binding protein or part of a DNA-binding complex that recognizes the UASs of both PUT1 and PUT2 [6].

Regulatory relationships of PUT3

  • We report that Gal4p can activate the PUT structural genes in a strain lacking Put3p [11].

Other interactions of PUT3

  • The enzymes of the proline utilization pathway (the products of the PUT1 and PUT2 genes) in Saccharomyces cerevisiae are coordinately regulated by proline and the PUT3 transcriptional activator [12].
  • Here we show that a single UASNTR the unrelated cis-acting element was TTTGTTTAC situated upstream of GLN1, while in another the cis-acting element was the one previously shown to bind the PUT3 protein [13].
  • Treatment with rapamycin resulted in the hyperphosphorylation of Put3p, which was independent of Gln3p, Nil1p, and Ure2p [14].

Analytical, diagnostic and therapeutic context of PUT3

  • To understand how PUT3 is converted from an inactive to an active state, a dissection of its functional domains has been undertaken [9].


  1. Functional replacement of the carboxy-terminal two-thirds of the influenza A virus NS1 protein with short heterologous dimerization domains. Wang, X., Basler, C.F., Williams, B.R., Silverman, R.H., Palese, P., García-Sastre, A. J. Virol. (2002) [Pubmed]
  2. Modulation of transcription factor function by an amino acid: activation of Put3p by proline. Sellick, C.A., Reece, R.J. EMBO J. (2003) [Pubmed]
  3. Identification and characterization of yeast mutants and the gene for a cruciform cutting endonuclease. Kleff, S., Kemper, B., Sternglanz, R. EMBO J. (1992) [Pubmed]
  4. Structure of a HAP1-DNA complex reveals dramatically asymmetric DNA binding by a homodimeric protein. King, D.A., Zhang, L., Guarente, L., Marmorstein, R. Nat. Struct. Biol. (1999) [Pubmed]
  5. Structure and mobility of the PUT3 dimer. Walters, K.J., Dayie, K.T., Reece, R.J., Ptashne, M., Wagner, G. Nat. Struct. Biol. (1997) [Pubmed]
  6. The Saccharomyces cerevisiae PUT3 activator protein associates with proline-specific upstream activation sequences. Siddiqui, A.H., Brandriss, M.C. Mol. Cell. Biol. (1989) [Pubmed]
  7. Analysis of constitutive and noninducible mutations of the PUT3 transcriptional activator. Marczak, J.E., Brandriss, M.C. Mol. Cell. Biol. (1991) [Pubmed]
  8. Evidence for positive regulation of the proline utilization pathway in Saccharomyces cerevisiae. Brandriss, M.C. Genetics (1987) [Pubmed]
  9. Functional analysis of the PUT3 transcriptional activator of the proline utilization pathway in Saccharomyces cerevisiae. des Etages, S.A., Falvey, D.A., Reece, R.J., Brandriss, M.C. Genetics (1996) [Pubmed]
  10. Mutation of a phosphorylatable residue in Put3p affects the magnitude of rapamycin-induced PUT1 activation in a Gat1p-dependent manner. Leverentz, M.K., Campbell, R.N., Connolly, Y., Whetton, A.D., Reece, R.J. J. Biol. Chem. (2009) [Pubmed]
  11. Cross-pathway regulation in Saccharomyces cerevisiae: activation of the proline utilization pathway by Ga14p in vivo. D'Alessio, M., Brandriss, M.C. J. Bacteriol. (2000) [Pubmed]
  12. Isolation of constitutive mutations affecting the proline utilization pathway in Saccharomyces cerevisiae and molecular analysis of the PUT3 transcriptional activator. Marczak, J.E., Brandriss, M.C. Mol. Cell. Biol. (1989) [Pubmed]
  13. UASNTR functioning in combination with other UAS elements underlies exceptional patterns of nitrogen regulation in Saccharomyces cerevisiae. Rai, R., Daugherty, J.R., Cooper, T.G. Yeast (1995) [Pubmed]
  14. Rapamycin treatment results in GATA factor-independent hyperphosphorylation of the proline utilization pathway activator in Saccharomyces cerevisiae. Saxena, D., Kannan, K.B., Brandriss, M.C. Eukaryotic Cell (2003) [Pubmed]
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