Disease relevance of PGD1

• We have purified a His(6) tagged version of Hrs1p protein from E. coli and have obtained specific anti-Hrs1p polyclonal antibodies [1].

High impact information on PGD1

• Hence, the Gal11p/Med2p/Pgd1p triad may contribute to TBP recruitment independently of the rest of mediator [2].
• Thus, the Gal11p/Med2p/Pgd1p triad is both necessary for recruitment of intact mediator and appears to be sufficient for recruitment by Gcn4p as a free subcomplex [2].
• Second, mutation of pgd1 causes partial disruption of the Sin4 complex and leads to a defect in transcription reinitiation [3].
• Hrs1p/Mcp6p on the meiotic SPB organizes astral microtubule arrays for oscillatory nuclear movement [4].
• Hrs1p interacted with components of the gamma-tubulin ring complex (gamma-TuRC) as well as with a meiotic SPB component [4].

Biological context of PGD1

• We provide genetic evidence that HRS1/PGD1, a yeast gene previously identified as a suppressor of the hyper-recombination phenotype of hpr1, has positive and negative roles in transcriptional regulation [5].
• Our results suggest that Hrs1p is required for the formation of deletions between direct repeats and that it may function in gene expression [1].
• We have cloned, sequenced and deleted from the genome the HRS1 gene [1].
• In addition, Hrs1p was required for mating-factor expression, telomere-linked DNA silencing and DNA supercoiling of plasmids [5].
• The DNA sequence of the HRS1 gene reveals that it is identical to PGD1, a gene with no reported function, and that the Hrs1p protein contains polyglutamine stretches typically found in transcription factors [1].

Anatomical context of PGD1

• Furthermore, hrs1 delta cells show reduced induction of the GAL1,10 promoter relative to wild-type cells [1].

Associations of PGD1 with chemical compounds

• The yeast HRS1 gene encodes a polyglutamine-rich nuclear protein required for spontaneous and hpr1-induced deletions between direct repeats [1].
• Finally, artificial holoenzyme recruitment assays support a model by which the contact between the corepressor and the Hrs1/Mediator may prevent pol II holoenzyme recruitment to the core promoter [6].
• Two-hybrid and glutathione S-transferase interaction assays show that Hrs1 can associate directly with Cyc8-Tup1 [6].

Regulatory relationships of PGD1

• RESULTS: Fusions with Med2 or Pgd1 activated CUP1 independently of TFIIE [7].

Other interactions of PGD1

• The hrs1 delta null mutation reduces the frequency of deletions in wild-type and hpr1 delta backgrounds sevenfold below wild-type and rad52 levels [1].

Analytical, diagnostic and therapeutic context of PGD1

• We show that Hrs1p is a 49-kD nuclear protein, as determined by indirect immunofluorescence microscopy and Western blot analysis [1].

References