TABLE 1.
Candidates for “receptors” with selectivity for 5-InsP7
| Systematic name | Gene name | Description |
|---|---|---|
| YDL083C | RPS16B | Component of the small (40S) ribosomal subunit |
| YGL252C | RTG2 | Sensor of mitochondrial dysfunction |
| YCL043C | PDI1 | Protein disulfide isomerase |
| YPR074C | TKL1 | Transketolase (in the pentose phosphate pathay) |
| YLR293C | GSP1 | Ran GTPase |
| YBR221C | PDB1 | E1 beta subunit of the pyruvate dehydrogenase (PDH) complex |
| YGL202W | ARO8 | Aromatic aminotransferase I |
| YER126C | NSA2 | Constituent of 66S pre-ribosomal particles |
| YJR063W | RPA12 | RNA polymerase I subunit A12.2 |
| YIL051C | MMF1 | Mitochondrial protein required for transamination of isoleucine |
| YCR053W | THR4 | Threonine synthase |
| YPL127C | HHO1 | Histone H1; linker histone with roles in meiosis and sporulation |
| YOL109W | ZEO1 | Peripheral membrane protein of the plasma membrane |
| YLR058C | SHM2 | Cytosolic serine hydroxymethyltransferase |
| YIL078W | THS1 | Threonyl-tRNA synthetase |
| YGL245W | GUS1 | Glutamyl-tRNA synthetase |
| YLR043C | TRX1 | Cytoplasmic thioredoxin isoenzyme |
| YLR083C | EMP70 | Protein with roles in cellular adhesion, filamentous growth and endosome-to- vacuole sorting |
| YDL185W | VMA1 | Subunit A of the V1 peripheral membrane domain of V-ATPase |
| YKL056C | TMA19 | Ribosome-associated protein |
| YGR124W | ASN2 | Asparagine synthetase |
| YLR109W | AHP1 | Thiol-specific peroxiredoxin |
The listed genes (as described in the Saccharomyces genome database, http://www.yeastgenome.org/) encode proteins in S. cerevisiae cell-lysates that were found to bind to a bead-immobilized, non-hydrolyzable, 5-bisphosphonate analogue of 5-InsP7 (5-PCP-InsP5) with >2-fold enrichment compared to binding to bead-immobilized InsP6 (Wu et al., 2016). Not listed are proteins that have CK2-consensus phosphorylation sites (and hence are candidates for PP-InsP mediated pyrophosphor-ylation); these were filtered out using Scansite, with medium stringency (http://scansite3.mit.edu/#home). Those proteins that remain may be considered as potentially hosting new examples of PP-InsP-specific, non-covalent binding domains. An important caveat is that there has not been a direct demonstration of direct binding of a PP-InsP to any of these candidates; any protein in this list could be pulled down through its association with another PP-InsP-binding protein. The author is grateful to Dr. Dorothea Fiedler for providing the information presented in this table.