The Mu Three-Site Synapse: A Strained Assembly Platform in which Delivery of the L1 Transposase Binding Site Triggers Catalytic Commitment
The Mu DNA transposition reaction proceeds through a three-site synaptic complex (LER), including the two Mu ends and the transpositional enhancer. We show that the LER contains highly stressed DNA regions in the enhancer and in the L1 transposase binding site. We propose that the L1 site acts as th...
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Veröffentlicht in: | Molecular cell 2002-09, Vol.10 (3), p.659-669 |
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creator | Kobryn, Kerri Watson, Mark A Allison, Ron G Chaconas, George |
description | The Mu DNA transposition reaction proceeds through a three-site synaptic complex (LER), including the two Mu ends and the transpositional enhancer. We show that the LER contains highly stressed DNA regions in the enhancer and in the L1 transposase binding site. We propose that the L1 site acts as the keystone for assembly of a catalytically competent transpososome. Delivery of L1 through HU-mediated bending completes LER assembly, provides the trigger for necessary conformational transitions in transpososome formation, and allows target capture to occur. Relief of the stress at L1 and the enhancer may help drive Mu A tetramerization and engagement of the Mu ends by the transposase active site. |
doi_str_mv | 10.1016/S1097-2765(02)00596-8 |
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We show that the LER contains highly stressed DNA regions in the enhancer and in the L1 transposase binding site. We propose that the L1 site acts as the keystone for assembly of a catalytically competent transpososome. Delivery of L1 through HU-mediated bending completes LER assembly, provides the trigger for necessary conformational transitions in transpososome formation, and allows target capture to occur. Relief of the stress at L1 and the enhancer may help drive Mu A tetramerization and engagement of the Mu ends by the transposase active site.</description><identifier>ISSN: 1097-2765</identifier><identifier>EISSN: 1097-4164</identifier><identifier>DOI: 10.1016/S1097-2765(02)00596-8</identifier><identifier>PMID: 12408832</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Bacteriophage mu - enzymology ; Bacteriophage mu - genetics ; Binding Sites ; Catalysis ; Chromosome Pairing ; DNA - chemistry ; DNA - genetics ; DNA - metabolism ; DNA Footprinting ; DNA, Viral ; DNA-Binding Proteins - genetics ; DNA-Binding Proteins - metabolism ; Enhancer Elements, Genetic ; Nucleic Acid Conformation ; Protein Binding ; Transposases - genetics ; Transposases - metabolism ; Viral Proteins - genetics ; Viral Proteins - metabolism</subject><ispartof>Molecular cell, 2002-09, Vol.10 (3), p.659-669</ispartof><rights>2002 Cell Press</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S1097276502005968$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12408832$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kobryn, Kerri</creatorcontrib><creatorcontrib>Watson, Mark A</creatorcontrib><creatorcontrib>Allison, Ron G</creatorcontrib><creatorcontrib>Chaconas, George</creatorcontrib><title>The Mu Three-Site Synapse: A Strained Assembly Platform in which Delivery of the L1 Transposase Binding Site Triggers Catalytic Commitment</title><title>Molecular cell</title><addtitle>Mol Cell</addtitle><description>The Mu DNA transposition reaction proceeds through a three-site synaptic complex (LER), including the two Mu ends and the transpositional enhancer. We show that the LER contains highly stressed DNA regions in the enhancer and in the L1 transposase binding site. We propose that the L1 site acts as the keystone for assembly of a catalytically competent transpososome. Delivery of L1 through HU-mediated bending completes LER assembly, provides the trigger for necessary conformational transitions in transpososome formation, and allows target capture to occur. Relief of the stress at L1 and the enhancer may help drive Mu A tetramerization and engagement of the Mu ends by the transposase active site.</description><subject>Bacteriophage mu - enzymology</subject><subject>Bacteriophage mu - genetics</subject><subject>Binding Sites</subject><subject>Catalysis</subject><subject>Chromosome Pairing</subject><subject>DNA - chemistry</subject><subject>DNA - genetics</subject><subject>DNA - metabolism</subject><subject>DNA Footprinting</subject><subject>DNA, Viral</subject><subject>DNA-Binding Proteins - genetics</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>Enhancer Elements, Genetic</subject><subject>Nucleic Acid Conformation</subject><subject>Protein Binding</subject><subject>Transposases - genetics</subject><subject>Transposases - metabolism</subject><subject>Viral Proteins - genetics</subject><subject>Viral Proteins - metabolism</subject><issn>1097-2765</issn><issn>1097-4164</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU2P0zAQhi0EYpeFnwDyCS2HwPgjTsIFdcvHrlQEUsPZcuxJa5Q4xXYX5S_wq2m75cxpXo0evdLMQ8hLBm8ZMPVuzaCpCl6p8hr4G4CyUUX9iFye1pIp-ficj8gFeZbSTwAmy7p5Si4Yl1DXgl-SP-0W6dc9bbcRsVj7jHQ9B7NL-J4u6DpH4wM6ukgJx26Y6ffB5H6KI_WB_t56u6UfcfD3GGc69TQfylaMttGEtJuSSUhvfHA-bOipuo1-s8GY6NJkM8zZW7qcxtHnEUN-Tp70Zkj44jyvyI_Pn9rlbbH69uVuuVgVyBuZCwesrJypBFON4w46J42olbXOSNWBUKzpLeO16psebQfGOF4yDo0VwqgKxRV5_dC7i9OvPaasR58sDoMJOO2TrriSqhblf0FWlwKkgAP46gzuuxGd3kU_mjjrf28-AB8eADzcde8x6mQ9BovOR7RZu8lrBvooVp_E6qM1DVyfxOpa_AUvZ5Tu</recordid><startdate>20020901</startdate><enddate>20020901</enddate><creator>Kobryn, Kerri</creator><creator>Watson, Mark A</creator><creator>Allison, Ron G</creator><creator>Chaconas, George</creator><general>Elsevier Inc</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7TM</scope><scope>7X8</scope></search><sort><creationdate>20020901</creationdate><title>The Mu Three-Site Synapse: A Strained Assembly Platform in which Delivery of the L1 Transposase Binding Site Triggers Catalytic Commitment</title><author>Kobryn, Kerri ; Watson, Mark A ; Allison, Ron G ; Chaconas, George</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-e294t-d0157da73169d2d0bd4a386ccda46b03619fc1286f9fecb0aad251209c33a67e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Bacteriophage mu - enzymology</topic><topic>Bacteriophage mu - genetics</topic><topic>Binding Sites</topic><topic>Catalysis</topic><topic>Chromosome Pairing</topic><topic>DNA - chemistry</topic><topic>DNA - genetics</topic><topic>DNA - metabolism</topic><topic>DNA Footprinting</topic><topic>DNA, Viral</topic><topic>DNA-Binding Proteins - genetics</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>Enhancer Elements, Genetic</topic><topic>Nucleic Acid Conformation</topic><topic>Protein Binding</topic><topic>Transposases - genetics</topic><topic>Transposases - metabolism</topic><topic>Viral Proteins - genetics</topic><topic>Viral Proteins - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kobryn, Kerri</creatorcontrib><creatorcontrib>Watson, Mark A</creatorcontrib><creatorcontrib>Allison, Ron G</creatorcontrib><creatorcontrib>Chaconas, George</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>Nucleic Acids Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Molecular cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kobryn, Kerri</au><au>Watson, Mark A</au><au>Allison, Ron G</au><au>Chaconas, George</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The Mu Three-Site Synapse: A Strained Assembly Platform in which Delivery of the L1 Transposase Binding Site Triggers Catalytic Commitment</atitle><jtitle>Molecular cell</jtitle><addtitle>Mol Cell</addtitle><date>2002-09-01</date><risdate>2002</risdate><volume>10</volume><issue>3</issue><spage>659</spage><epage>669</epage><pages>659-669</pages><issn>1097-2765</issn><eissn>1097-4164</eissn><abstract>The Mu DNA transposition reaction proceeds through a three-site synaptic complex (LER), including the two Mu ends and the transpositional enhancer. We show that the LER contains highly stressed DNA regions in the enhancer and in the L1 transposase binding site. We propose that the L1 site acts as the keystone for assembly of a catalytically competent transpososome. Delivery of L1 through HU-mediated bending completes LER assembly, provides the trigger for necessary conformational transitions in transpososome formation, and allows target capture to occur. Relief of the stress at L1 and the enhancer may help drive Mu A tetramerization and engagement of the Mu ends by the transposase active site.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>12408832</pmid><doi>10.1016/S1097-2765(02)00596-8</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Bacteriophage mu - enzymology Bacteriophage mu - genetics Binding Sites Catalysis Chromosome Pairing DNA - chemistry DNA - genetics DNA - metabolism DNA Footprinting DNA, Viral DNA-Binding Proteins - genetics DNA-Binding Proteins - metabolism Enhancer Elements, Genetic Nucleic Acid Conformation Protein Binding Transposases - genetics Transposases - metabolism Viral Proteins - genetics Viral Proteins - metabolism |
title | The Mu Three-Site Synapse: A Strained Assembly Platform in which Delivery of the L1 Transposase Binding Site Triggers Catalytic Commitment |
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