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Published on: September 28, 2017
Structure and DNA binding of the human Rtf1 Plus3 domain
Rob N de Jong1, Vincent Truffault, Tammo Diercks
1Bijvoet Centre for Biomolecular Research, Utrecht University, Faculty of Chemistry, Department NMR Spectroscopy, Padualaan 8, Utrecht, The Netherlands.
Structure (London, England : 1993)
|January 11, 2008
Summary
The Rtf1 Plus3 domain
Area of Science:
- Molecular Biology
- Biochemistry
- Structural Biology
Background:
- The Paf1 complex is crucial for regulating gene expression through histone modifications and RNA processing.
- Key components include Paf1, Rtf1, Cdc73, Ctr9, and Leo1.
Purpose of the Study:
- To elucidate the structure of the conserved Rtf1 Plus3 domain.
- To investigate the DNA/RNA binding capabilities of the Rtf1 Plus3 domain.
- To explore the potential role of Rtf1 Plus3 in transcription.
Main Methods:
- Nuclear Magnetic Resonance (NMR) spectroscopy was used to determine the structure of the Rtf1 Plus3 domain.
- In vitro biochemical assays were performed to assess DNA and RNA binding.
- Structural comparisons were made with known protein domains like PAZ and Tudor.
Main Results:
- The Rtf1 Plus3 domain adopts a predominantly beta-stranded structure.
- This structure exhibits similarity to Dicer/Argonaute PAZ and Tudor domains.
- The Rtf1 Plus3 domain specifically binds single-stranded DNA (ssDNA) in vitro.
- No binding to double-stranded DNA (dsDNA) or RNA was detected.
Conclusions:
- The Rtf1 Plus3 domain's structure provides insight into its function within the Paf1 complex.
- The ssDNA binding capability suggests a role in regulating transcription elongation.
- This interaction may be mediated by basic residues on the beta sheet rim.
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