This study used the yeast two-hybrid system to identify novel proteins interacting with the orphan receptor RVR. Two gene products were pulled out of two independent screens. We named them L5B and RVRin62. The RVRint62 was characterized in this research. RVRint62 is a partial cDNA clone of approximately 2.2 kb, which is expressed in most tissues. It interacts with both members of the RVR/Rev-erb$ alpha$ subfamily of the nuclear receptor superfamily. The domains of RVR responsible for the interaction with RVRint62 were characterized as the C-terminal of the LBD and the signature motif. The interaction domain of RVRint62 is situated in the first 300 amino acids of its N-terminus. The motif LXXLL, found in many co-regulatory proteins that interact with nuclear receptors, is also found in RVRint62. However, the LXXLL motif is not required for interaction with RVR. The potential modulating role of RVRint62 on RVR activity remains to be determined.
| Identifer | oai:union.ndltd.org:LACETR/oai:collectionscanada.gc.ca:QMM.27523 |
| Date | January 1997 |
| Creators | Gallant, Josette. |
| Contributors | Giguere, Vincent (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 Biochemistry.) |
| Rights | All items in eScholarship@McGill are protected by copyright with all rights reserved unless otherwise indicated. |
| Relation | alephsysno: 001751998, proquestno: MQ37121, Theses scanned by UMI/ProQuest. |
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