Regulators of G protein signaling (RGS) are proteins that negatively regulate G protein-coupled receptor signaling. Although a conserved core domain is necessary and sufficient for their GTPase accelerating protein (GAP) activity, many RGSs possess C- and N-terminal protein-binding motifs that augment GAP activity and participate in other cellular regulatory mechanisms. / Human RGS 1 functionally complements a Saccharomyces cerevisiae mutant lacking the RGS homologue Sst2p. We demonstrate that deletion of the N-terminus or RGS domain negatively affects this ability in Sst2p-deficient strains, whereas deletion of the C-terminal 10 residues of RGS 1 does not. Coexpression of the N-terminus and RGS domains restores complementation of Sst2p to that of wild type. The conservative replacement of sequential residues spanning the N-terminus of RGS1 causes little loss of function. These results suggest that the N-terminal and RGS domains of RGS I function in concert to effect signaling and that the C-terminal 10 residues of RGS I are not required for this activity. Further, residues present in the N-terminus are not highly conserved suggesting that overall structure, rather than individual residues or motifs, may be important for function.
| Identifer | oai:union.ndltd.org:LACETR/oai:collectionscanada.gc.ca:QMM.33845 |
| Date | January 2002 |
| Creators | Somerville, Wendy. |
| Contributors | Greenwood, M. (advisor) |
| Publisher | McGill University |
| Source Sets | Library and Archives Canada ETDs Repository / Centre d'archives des thèses électroniques de Bibliothèque et Archives Canada |
| Language | English |
| Detected Language | English |
| Type | Electronic Thesis or Dissertation |
| Format | application/pdf |
| Coverage | Master of Science (Department of Anatomy and Cell Biology.) |
| Rights | All items in eScholarship@McGill are protected by copyright with all rights reserved unless otherwise indicated. |
| Relation | alephsysno: 001863633, proquestno: MQ78962, Theses scanned by UMI/ProQuest. |
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