Table 1.
Cytoplasmic loop of Catsup interacts physically with TH and GTPCH in a yeast two hybrid assay1
| Catsup Loop2 | TH Fragments3 | SD(-T,-W,-H) | LacZ |
|---|---|---|---|
| Full-length | Full-length | + | + |
| C-terminal domain | Full-length | + | + |
| Full-length | N-terminal half | + | + |
| C-terminal domain | N-terminal half | + | + |
| Full-length | C-terminal half | − | − |
| C-terminal domain | C-terminal half | − | − |
| N-terminal domain | Full-length | − | − |
| Catsup Loop 1 | GTPCH Fragments 4 | SD(-T,-W,-H) | LacZ |
| C-terminal domain | Full-length GTPCHa/Pu-RA | + | + |
| C-terminal domain | N-terminal GTPCHa/Pu-RA | + | + |
| N-terminal domain | Full-length GTPCHa/Pu-RA | − | − |
| C-terminal domain | Full-length GTPCHc/Pu-RC | + | + |
| C-terminal domain | N-terminal GTPCHc/Pu-RC | + | + |
| N-terminal domain | Full-length GTPCHc/Pu-RC | − | − |
| C-terminal domain | GTPCH catalytic domain | − | − |
The full length Catsup cytoplasmic loop and its C-terminal and N-terminal halves in the pGAD-C1 vector were used as bait; prey constructs were the full length, N-terminal and C-terminal fragments of TH, and the full length protein and N-terminal regulatory and catalytic domain fragments of GTPCH isoforms RA and RC in the pGBD-C1 vector. (+): yeast cells grew on SD/-Trp-Ade-His plates and developed blue coloration after incubation with X-gal. (−): no growth on the selection medium.
Full length Catsup loop: residues 242-363; N-terminal fragment: residues 242- 295; C-terminal fragment: residues 293-363.
Full length TH: residues 1-508; N-terminal half: residues 1-269; C-terminal half: residues 269-508.
Full length GTPCHa/RA: residues 1-324; N-terminal GTPCHa/RA: residues 1-117. Full length GTPCHc/RC: residues 1-308; N-terminal GTPCHc/RC: residues 1-101. Catalytic domain (shared by GTPCH-RA and –RC): residues 118 in RA and 102 in RC to C- terminus.