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...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Molecular cell 2002-09, Vol.10 (3), p.659-669
Hauptverfasser: Kobryn, Kerri, Watson, Mark A, Allison, Ron G, Chaconas, George
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 669
container_issue 3
container_start_page 659
container_title Molecular cell
container_volume 10
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
format Article
fullrecord <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_proquest_miscellaneous_72646835</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S1097276502005968</els_id><sourcerecordid>18530430</sourcerecordid><originalsourceid>FETCH-LOGICAL-e294t-d0157da73169d2d0bd4a386ccda46b03619fc1286f9fecb0aad251209c33a67e3</originalsourceid><addsrcrecordid>eNqFkU2P0zAQhi0EYpeFnwDyCS2HwPgjTsIFdcvHrlQEUsPZcuxJa5Q4xXYX5S_wq2m75cxpXo0evdLMQ8hLBm8ZMPVuzaCpCl6p8hr4G4CyUUX9iFye1pIp-ficj8gFeZbSTwAmy7p5Si4Yl1DXgl-SP-0W6dc9bbcRsVj7jHQ9B7NL-J4u6DpH4wM6ukgJx26Y6ffB5H6KI_WB_t56u6UfcfD3GGc69TQfylaMttGEtJuSSUhvfHA-bOipuo1-s8GY6NJkM8zZW7qcxtHnEUN-Tp70Zkj44jyvyI_Pn9rlbbH69uVuuVgVyBuZCwesrJypBFON4w46J42olbXOSNWBUKzpLeO16psebQfGOF4yDo0VwqgKxRV5_dC7i9OvPaasR58sDoMJOO2TrriSqhblf0FWlwKkgAP46gzuuxGd3kU_mjjrf28-AB8eADzcde8x6mQ9BovOR7RZu8lrBvooVp_E6qM1DVyfxOpa_AUvZ5Tu</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>18530430</pqid></control><display><type>article</type><title>The Mu Three-Site Synapse: A Strained Assembly Platform in which Delivery of the L1 Transposase Binding Site Triggers Catalytic Commitment</title><source>MEDLINE</source><source>Cell Press Free Archives</source><source>Elsevier ScienceDirect Journals</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>Free Full-Text Journals in Chemistry</source><creator>Kobryn, Kerri ; Watson, Mark A ; Allison, Ron G ; Chaconas, George</creator><creatorcontrib>Kobryn, Kerri ; Watson, Mark A ; Allison, Ron G ; Chaconas, George</creatorcontrib><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><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>
fulltext fulltext
identifier ISSN: 1097-2765
ispartof Molecular cell, 2002-09, Vol.10 (3), p.659-669
issn 1097-2765
1097-4164
language eng
recordid cdi_proquest_miscellaneous_72646835
source MEDLINE; Cell Press Free Archives; Elsevier ScienceDirect Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Free Full-Text Journals in Chemistry
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
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-02T14%3A42%3A26IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=The%20Mu%20Three-Site%20Synapse:%20A%20Strained%20Assembly%20Platform%20in%20which%20Delivery%20of%20the%20L1%20Transposase%20Binding%20Site%20Triggers%20Catalytic%20Commitment&rft.jtitle=Molecular%20cell&rft.au=Kobryn,%20Kerri&rft.date=2002-09-01&rft.volume=10&rft.issue=3&rft.spage=659&rft.epage=669&rft.pages=659-669&rft.issn=1097-2765&rft.eissn=1097-4164&rft_id=info:doi/10.1016/S1097-2765(02)00596-8&rft_dat=%3Cproquest_pubme%3E18530430%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=18530430&rft_id=info:pmid/12408832&rft_els_id=S1097276502005968&rfr_iscdi=true