Pub1p C-Terminal RRM Domain Interacts with Tif4631p through a Conserved Region Neighbouring the Pab1p Binding Site
2011
Study of Pub1p Protein Interactions and Structure
publication
Evidence: high
Author Information
Author(s): Clara M. Santiveri, Yasmina Rico-Lastres, Palma Martínez-Lumbreras, Santiago Pérez-Cañadillas, José Manuel Tuite
Primary Institution: Instituto de Química-Física “Rocasolano”, CSIC, Madrid, Spain
Hypothesis
How does the C-terminal RRM domain of Pub1p interact with Tif4631p and RNA?
Conclusion
The study reveals that Pub1p's C-terminal RRM domain interacts specifically with Tif4631p and binds RNA with high selectivity for U-rich sequences.
Supporting Evidence
- Pub1p binds RNA with high selectivity for U-rich sequences.
- The C-terminal RRM domain of Pub1p shows a novel structural feature.
- Pub1p interacts specifically with the N-terminal region of Tif4631p.
- The interaction involves conserved residues of Pub1p TRRM.
Takeaway
This research looks at how a protein called Pub1p interacts with another protein and RNA, which helps control how genes are expressed in cells.
Methodology
The study utilized NMR spectroscopy to analyze the structure and interactions of Pub1p with RNA and Tif4631p.
Digital Object Identifier (DOI)
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