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Transient DNA/RNA-protein interactions.
FEBS J. 2011 May; 278(10):1643-50
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03 Aug 2011
Richard Lavery
F1000 Structural Biology
Institute of Biology and Chemistry of Proteins,
Lyon, France.
F1000 Structural Biology
Institute of Biology and Chemistry of Proteins,
Lyon, France.
Review / Commentary
DOI: 10.3410/f.12409957.13609056
Transient protein-nucleic acid interactions are vital for living organisms, notably playing major roles in the regulation of replication and transcription, translation and nucleosome positioning. However, the transient nature of these interactions limits the structural information presently available....Continue reading
Transient protein-nucleic acid interactions are vital for living organisms, notably playing major roles in the regulation of replication and transcription, translation and nucleosome positioning. However, the transient nature of these interactions limits the structural information presently available. Compared to protein-protein interactions, protein-nucleic acid interactions are underrepresented in the Protein Data Bank (PDB) (~4%). Blanco and Montoya comment on the difficulties encountered in characterizing these structures and give an overview of the techniques applicable in this area.
While considerable progress in biotechnology and biomedicine would be made by rationally redesigning DNA-binding proteins, the authors note that this will require more structural information on protein-DNA complexes and also a deeper understanding of indirect readout mechanisms.
While considerable progress in biotechnology and biomedicine would be made by rationally redesigning DNA-binding proteins, the authors note that this will require more structural information on protein-DNA complexes and also a deeper understanding of indirect readout mechanisms.
Disclosures
None declared
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Lavery R and Pérez A: F1000Prime Recommendation of [Blanco FJ and Montoya G, FEBS J 2011, 278(10):1643-50]. In F1000Prime, 03 Aug 2011; DOI: 10.3410/f.12409957.13609056. F1000Prime.com/12409957#eval13609056
F1000Prime Recommendations, Dissents and Comments for [Blanco FJ and Montoya G, FEBS J 2011, 278(10):1643-50]. In F1000Prime, 20 May 2013; F1000Prime.com/12409957
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The great pace of biomolecular structure determination has provided a plethora of protein structures, but not as many structures of nucleic acids or of their complexes with proteins. The recognition of DNA and RNA molecules by proteins may produce large and relatively stable assemblies (such as the ribosome) or transient complexes (such as DNA clamps sliding through the DNA). These transient interactions are most difficult to characterize, but even in 'stable' complexes captured in crystal structures, the dynamics of the whole or part of the assembly pose great technical difficulties in understanding their function. The development and refinement of powerful experimental and computational tools have made it possible to learn a great deal about the relevance of these fleeting events for numerous biological processes. We discuss here the most recent findings and the challenges that lie ahead in the quest for a better understanding of protein-nucleic acid interactions.
© 2011 The Authors Journal compilation © 2011 FEBS.
DOI: 10.1111/j.1742-4658.2011.08095.x
PMID: 21410646
