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Saccharomyces cerevisiae Rbg1 protein and its binding partner Gir2 interact on Polyribosomes with Gcn1
P K Wout1, E Sattlegger, S M Sullivan
1Department of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, Michigan 48109-1048, USA.
Eukaryotic Cell
|May 19, 2009
Summary
Rbg1, a novel GTP-binding protein in Saccharomyces cerevisiae, associates with translating ribosomes. It interacts with Gir2, a protein involved in amino acid control, suggesting a role in ribosome function and cellular stress response.
Area of Science:
- Molecular Biology
- Cell Biology
- Yeast Genetics
Background:
- Rbg1 is a novel GTP-binding protein in Saccharomyces cerevisiae.
- It belongs to the Obg/CgtA subfamily, known for roles in ribosome function.
- Members of this subfamily are conserved across prokaryotes and eukaryotes.
Purpose of the Study:
- To characterize the function and interactions of the uncharacterized protein Rbg1.
- To investigate Rbg1's association with ribosomes.
- To identify proteins interacting with Rbg1 and explore their functional significance.
Main Methods:
- Yeast two-hybrid screening to identify Rbg1 interacting proteins.
- Co-fractionation studies with polyribosomes.
- Overexpression studies under conditions mimicking amino acid starvation.
Main Results:
- Rbg1 specifically associates with translating ribosomes.
- Proteins interacting with Rbg1 include Tma46, Ygr250c, Yap1, and Gir2.
- Gir2, containing a GI domain, interacts with Gcn1 and cofractionates with polyribosomes, with its function influenced by Gcn1 and Rbg1.
Conclusions:
- Rbg1 and its interacting partner Gir2 associate with ribosomes.
- These proteins likely play roles in ribosome function and cellular response to amino acid availability.
- Further investigation into their specific biological roles is warranted.
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