Pub. Date : 1994 Apr 1
PMID : 8144571
7 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
1 | Cis-acting sequences that modulate ENO1 URS (upstream repression site) element activity were identified by base pair substitution mutagenesis. | Peptichemio | phosphopyruvate hydratase ENO1 | Saccharomyces cerevisiae S288C |
2 | A binding site for the yeast REB1 protein was identified near the 5" terminus of the ENO1 URS element. | Peptichemio | phosphopyruvate hydratase ENO1 | Saccharomyces cerevisiae S288C |
3 | Base substitution mutations within a second region of the ENO1 URS element caused a 38% loss of URS activity in vivo. | Peptichemio | phosphopyruvate hydratase ENO1 | Saccharomyces cerevisiae S288C |
4 | Base substitution mutations within a second region of the ENO1 URS element caused a 38% loss of URS activity in vivo. | Peptichemio | phosphopyruvate hydratase ENO1 | Saccharomyces cerevisiae S288C |
5 | Base substitution mutations within a third region near the 3" terminus of the ENO1 URS element caused a 70% loss of URS activity in vivo. | Peptichemio | phosphopyruvate hydratase ENO1 | Saccharomyces cerevisiae S288C |
6 | Base substitution mutations within a third region near the 3" terminus of the ENO1 URS element caused a 70% loss of URS activity in vivo. | Peptichemio | phosphopyruvate hydratase ENO1 | Saccharomyces cerevisiae S288C |
7 | These results showed that ENO1 URS element activity was modulated by multiple cis-acting sequences that bound distinct trans-acting factors. | Peptichemio | phosphopyruvate hydratase ENO1 | Saccharomyces cerevisiae S288C |