期刊
JOURNAL OF MOLECULAR BIOLOGY
卷 367, 期 2, 页码 319-327出版社
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2006.12.064
关键词
transposition; transposase; Tn5; protein-nucleic acid interactions; single molecule
资金
- NIGMS NIH HHS [GM71019, GM50692] Funding Source: Medline
- Division Of Physics
- Direct For Mathematical & Physical Scien [0852130] Funding Source: National Science Foundation
The Tn5 transposase is an example of a class of proteins that move DNA sequences (transposons) via a process called transposition. DNA transposition is a widespread genetic mobility mechanism that has profoundly affected the genomes of nearly all organisms. We have used single-DNA micromanipulation experiments to study the process by which Tn5 DNA transposons are identified and processed by their transposase protein. We have determined that the energy barrier to disassemble catalytically active synaptic complexes is 16 kcal mol(-1). However, we have found that the looping organization of DNA segments by transposase is less sequence-driven than previously thought. Loops anchored at some non-transposon end sequences display a disassembly energy barrier of 14 kcal mol(-1), nearly as stable as the synapses formed at known transposon end sequences. However, these non-transposon end sequence independent complexes do not mediate DNA cleavage. Therefore, the sequence-sensitivity for DNA binding and looping by Tn5 transposase is significantly less than that required for DNA cleavage. These results have implications for the in vivo down regulation of transposition and the cis-transposition bias of transposase. (c) 2006 Elsevier Ltd. All rights reserved.
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