Disease relevance of PUT3

• Recombinant influenza viruses were generated that expressed truncated NS1 proteins of 126 amino acids, fused to 28 or 24 amino acids derived from the dimerization domains of either the Saccharomyces cerevisiae PUT3 or the Drosophila melanogaster Ncd (DmNcd) proteins [1].

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

• The Saccharomyces cerevisiae PUT3 activator protein associates with proline-specific upstream activation sequences [6].
• PUT3 (31-100) contains three distinct domains: a cysteine zinc cluster, linker, and dimerization domain [5].
• PUT3, the activator of the proline utilization pathway, is required for the transcription of the genes encoding the enzymes that convert proline to glutamate [9].
• We find that the mutation of Put3p at amino acid Tyr-788 modulates the proline-independent activation of PUT1 through Gat1p [10].

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].

References