Exploring translocation of proteins on DNA by NMR

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• 作者：G. Marius Clore (1) mariusc@mail.nih.gov
• 关键词：Protein ; DNA interactions – ; Sliding – ; Direct transfer – ; Target search process – ; Paramagnetic relaxation enhancement – ; z ; Exchange spectroscopy – ; Lineshape analysis
• 刊名：Journal of Biomolecular NMR
• 出版年：2011
• 出版时间：November 2011
• 年：2011
• 卷：51
• 期：3
• 页码：209-219
• 全文大小：2.2 MB
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• 作者单位：1. Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 02892-0520, USA
• 刊物类别：Physics and Astronomy
• 刊物主题：Physics
  Biophysics and Biomedical Physics
  Polymer Sciences
  Biochemistry
  
• 出版者：Springer Netherlands
• ISSN：1573-5001

文摘

While an extensive body of knowledge has accumulated on the structures of transcription factors, DNA and their complexes from both NMR and crystallography, much less is known at a molecular level regarding the mechanisms whereby transcription factors locate their specific DNA target site within an overwhelming sea of non-specific DNA sites. Indirect kinetic data suggested that three processes are involved in the search procedure: jumping by dissociation of the protein from the DNA followed by re-association at another site, direct transfer from one DNA molecule or segment to another, and one-dimensional sliding. In this brief perspective I summarize recent NMR developments from our laboratory that have permitted direct characterization of the species and molecular mechanisms involved in the target search process, including the detection of highly transient sparsely-populated states. The main tool in these studies involves the application of paramagnetic relaxation enhancement, supplemented by z-exchange spectroscopy, lineshape analysis and residual dipolar couplings. These studies led to the first direct demonstration of rotation-coupled sliding of a protein along the DNA and the direct transfer of a protein from one DNA molecule to another without dissociating into free solution.