Project information
Structural studies of protein-RNA complexes involved in RNA quality control
- Project Identification
- LA08008
- Project Period
- 1/2008 - 12/2010
- Investor / Pogramme / Project type
-
Ministry of Education, Youth and Sports of the CR
- INGO
- MU Faculty or unit
- Faculty of Science
- Keywords
- RNA quality control; misfolded RNA; RNA turnover; RNA recognition; protein-RNA complexes; structure; nuclear magnetic resonance
Cells seem to leave nothing to chance, including the quality control at all steps of information transfer. RNA maturation involves extensive processing that has a relatively high error rate. Cells have developed an RNA quality control mechanism which identifies improperly processed RNAs and subsequently degrades them. This mechanism ensures that only properly processed RNAs are engaged in protein synthesis. The exosome and Trf4 complex are the central molecular machines in this process. The Trf4 complex recognizes and polyadenylates the aberrant RNAs, whereas the exosome is responsible for their degradation. We propose here to use multidimensional NMR spectroscopy to determine the three-dimensional structure of several protein-RNA complexes that are involved in RNA quality control. The proposed project will reveal the mechanism by which the Trf4 complex identifies the aberrant RNAs and thus recruit them for the degradation machinery.
Publications
Total number of publications: 10
2011
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1H, 13C, and 15N resonance assignments for the CTD-Interacting Domain of Nrd1 bound to Ser5-phosphorylated CTD of RNA Polymerase II
Biomolecular NMR Assignments, year: 2011, volume: 5, edition: 2, DOI
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Recognition of transcription termination signal by the nuclear polyadenylated RNA-binding (Nab)3 protein
The Journal of Biological Chemistry, year: 2011, volume: 286, edition: 5, DOI
2010
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(1)H, (13)C, and (15)N chemical shift assignments for the RNA recognition motif of Nab3.
Biomolecular NMR Assignments, year: 2010, volume: 4, edition: 1, DOI
-
1H, 13C, and 15N chemical shift assignments of ZCCHC9
Biomolecular NMR Assignments, year: 2010, volume: 5, edition: 1, DOI
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The computational view inside the dynamical behavior of the RNA-binding motive
Year: 2010, type: Conference abstract
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The Solution Structure of the ADAR2 dsRBM-RNA Complex Reveals a Sequence-Specific Readout of the Minor Groove
CELL, year: 2010, volume: 143, edition: 2
2009
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Recognition of phosphorylated CTD of RNA Pol II by Nrd1
Year: 2009, type: Conference abstract
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Structure and RNA binding of Nab3
Year: 2009, type: Conference abstract
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The molecular dynamics study of the RNA-binding domain of ADAR2 bound to dsRNA
Year: 2009, type: Conference abstract
-
Transcription termination of nonpolyadenylated transcripts
Year: 2009, type: Conference abstract