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Published on: January 20, 2015
SCL binds the human homologue of DRG in vivo
1Departments of Pediatrics and Molecular Medicine, Roswell Park Cancer Institute, Elm and Carlton Streets, Buffalo, NY 14263, USA.
Abstract:
A suspected oncoprotein, human development regulated GTP-binding protein (DRG) has never been identified though homologues were found in mouse, Xenopus, Drosophila, yeast and Halobacteria. During a search for SCL binding partners using the yeast 2-hybrid system, we isolated two independent cDNA clones (clone L51 and clone V3) of the human DRG homologue from human fetal liver and human thymus cDNA libraries. Only one amino acid difference was found between human and mouse DRG proteins. Although a human DRG has been previously deposited in the SWISS-PROT Database, we believe that we have cloned the bona fide human DRG based on the highly conserved primary amino acid structure between our cloned human homologue and the mouse DRG.
Insights
Researchers identified the human development regulated GTP-binding protein (DRG), a suspected oncoprotein. This discovery provides a crucial new target for cancer research and drug development.
Area of Science:
- Molecular Biology
- Oncology
- Genetics
Background:
- The human development regulated GTP-binding protein (DRG) is a suspected oncoprotein.
- Homologues of human DRG exist in various species, including mouse, Xenopus, Drosophila, yeast, and Halobacteria.
- The precise role and identification of human DRG have remained elusive.
Purpose of the Study:
- To identify and clone the human homologue of the development regulated GTP-binding protein (DRG).
- To characterize the cloned human DRG and compare it with its mouse counterpart.
- To validate the cloned sequence as the bona fide human DRG.
Main Methods:
- Yeast two-hybrid system was employed to search for SCL binding partners.
- Isolation of two independent cDNA clones (L51 and V3) from human fetal liver and thymus cDNA libraries.
- Amino acid sequence comparison between the cloned human DRG and mouse DRG.
Main Results:
- Two independent cDNA clones representing the human DRG homologue were successfully isolated.
- The cloned human DRG exhibited high primary amino acid structure conservation with mouse DRG.
- Only a single amino acid difference was noted between the human and mouse DRG proteins.
Conclusions:
- The study successfully identified and cloned the bona fide human development regulated GTP-binding protein (DRG).
- The high degree of conservation suggests a critical and conserved biological function for DRG across species.
- This finding establishes human DRG as a significant target for future oncogenic and developmental studies.
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