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Detailed mechanism for transposition by TnpA transposase involves DNA shape rather than direct protein-DNA recognition to generate an active nucleoprotein complex
A series of single-crystal structures determined by Barabas and colleagues provides a detailed mechanism for how the TnpA transposase from Helicobacter pylori recognizes, cleaves, and integrates the IS200/IS605 class of transposable elements. An interesting aspect of the mechanism is that the transp...
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Formato: | Texto |
Lenguaje: | English |
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Biology Reports Ltd
2009
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2924686/ https://www.ncbi.nlm.nih.gov/pubmed/20948648 http://dx.doi.org/10.3410/B1-37 |
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author | Ho, P Shing |
author_facet | Ho, P Shing |
author_sort | Ho, P Shing |
collection | PubMed |
description | A series of single-crystal structures determined by Barabas and colleagues provides a detailed mechanism for how the TnpA transposase from Helicobacter pylori recognizes, cleaves, and integrates the IS200/IS605 class of transposable elements. An interesting aspect of the mechanism is that the transposase recognizes the transposon through the unique fold-back structure adopted by the sequences of the DNA components, rather than through direct protein-DNA interactions. This is an example of indirect readout that is reminiscent of how four-stranded junctions are recognized by recombination proteins, but is also analogous to ribonucleoproteins, in that the DNA facilitates formation of an active nucleic acid-protein complex. |
format | Text |
id | pubmed-2924686 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2009 |
publisher | Biology Reports Ltd |
record_format | MEDLINE/PubMed |
spelling | pubmed-29246862010-10-14 Detailed mechanism for transposition by TnpA transposase involves DNA shape rather than direct protein-DNA recognition to generate an active nucleoprotein complex Ho, P Shing F1000 Biol Rep Review Article A series of single-crystal structures determined by Barabas and colleagues provides a detailed mechanism for how the TnpA transposase from Helicobacter pylori recognizes, cleaves, and integrates the IS200/IS605 class of transposable elements. An interesting aspect of the mechanism is that the transposase recognizes the transposon through the unique fold-back structure adopted by the sequences of the DNA components, rather than through direct protein-DNA interactions. This is an example of indirect readout that is reminiscent of how four-stranded junctions are recognized by recombination proteins, but is also analogous to ribonucleoproteins, in that the DNA facilitates formation of an active nucleic acid-protein complex. Biology Reports Ltd 2009-05-08 /pmc/articles/PMC2924686/ /pubmed/20948648 http://dx.doi.org/10.3410/B1-37 Text en © 2009 Biology Reports Ltd http://creativecommons.org/licenses/by-nc/3.0/legalcode This is an open-access article distributed under the terms of the Creative Commons Attribution-Non Commercial License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. You may not use this work for commercial purposes |
spellingShingle | Review Article Ho, P Shing Detailed mechanism for transposition by TnpA transposase involves DNA shape rather than direct protein-DNA recognition to generate an active nucleoprotein complex |
title | Detailed mechanism for transposition by TnpA transposase involves DNA shape rather than direct protein-DNA recognition to generate an active nucleoprotein complex |
title_full | Detailed mechanism for transposition by TnpA transposase involves DNA shape rather than direct protein-DNA recognition to generate an active nucleoprotein complex |
title_fullStr | Detailed mechanism for transposition by TnpA transposase involves DNA shape rather than direct protein-DNA recognition to generate an active nucleoprotein complex |
title_full_unstemmed | Detailed mechanism for transposition by TnpA transposase involves DNA shape rather than direct protein-DNA recognition to generate an active nucleoprotein complex |
title_short | Detailed mechanism for transposition by TnpA transposase involves DNA shape rather than direct protein-DNA recognition to generate an active nucleoprotein complex |
title_sort | detailed mechanism for transposition by tnpa transposase involves dna shape rather than direct protein-dna recognition to generate an active nucleoprotein complex |
topic | Review Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2924686/ https://www.ncbi.nlm.nih.gov/pubmed/20948648 http://dx.doi.org/10.3410/B1-37 |
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