IS200/IS605 family single-strand transposition: mechanism of IS608 strand transfer
Transposase, TnpA, of the IS200/IS605 family member IS608, catalyses single-strand DNA transposition and is dimeric with hybrid catalytic sites composed of an HUH motif from one monomer and a catalytic Y127 present in an α-helix (αD) from the other (trans configuration). αD is attached to the main b...
Gespeichert in:
| Veröffentlicht in: | Nucleic acids research 2013-03, Vol.41 (5), p.3302-3313 |
|---|---|
| Hauptverfasser: | , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 3313 |
|---|---|
| container_issue | 5 |
| container_start_page | 3302 |
| container_title | Nucleic acids research |
| container_volume | 41 |
| creator | He, Susu Guynet, Catherine Siguier, Patricia Hickman, Alison B Dyda, Fred Chandler, Mick Ton-Hoang, Bao |
| description | Transposase, TnpA, of the IS200/IS605 family member IS608, catalyses single-strand DNA transposition and is dimeric with hybrid catalytic sites composed of an HUH motif from one monomer and a catalytic Y127 present in an α-helix (αD) from the other (trans configuration). αD is attached to the main body by a flexible loop. Although the reactions leading to excision of a transposition intermediate are well characterized, little is known about the dynamic behaviour of the transpososome that drives this process. We provide evidence strongly supporting a strand transfer model involving rotation of both αD helices from the trans to the cis configuration (HUH and Y residues from the same monomer). Studies with TnpA heterodimers suggest that TnpA cleaves DNA in the trans configuration, and that the catalytic tyrosines linked to the 5'-phosphates exchange positions to allow rejoining of the cleaved strands (strand transfer) in the cis configuration. They further imply that, after excision of the transposon junction, TnpA should be reset to a trans configuration before the cleavage required for integration. Analysis also suggests that this mechanism is conserved among members of the IS200/IS605 family. |
| doi_str_mv | 10.1093/nar/gkt014 |
| format | Article |
| fullrecord | <record><control><sourceid>pubmed_hal_p</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3597680</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>23345619</sourcerecordid><originalsourceid>FETCH-LOGICAL-h300t-75e92cadde8f3b7ce241c3e3448d094ab36aa22b17a95e2076c1e101f299397a3</originalsourceid><addsrcrecordid>eNpdkE9Lw0AQxRdRbK1e_ACyVw-xszub3awHoRS1hYJg9Rw2yaZZzZ-STQv99qZUpXqZgZnfe_MYQq4Z3DHQOK5NO159dsDECRkylDwQWvJTMgSEMGAgogG58P4DeoKF4pwMOKIIJdND8jpfcoDxfCkhpLmpXLmj3tWr0ga-a02d0X3168a7zjX1Pa1sWpja-Yo2Od3LInoM5ra9JGe5Kb29-u4j8v70-DadBYuX5_l0sggKBOgCFVrNU5NlNsoxUanlgqVoUYgoAy1MgtIYzhOmjA4tByVTZhmwnGuNWhkckYeD73qTVDZLbd0nKON16yrT7uLGuPjvpnZFvGq2MYZayQh6g9uDQfFPNpss4v0M-hxSod6ynr05PvaL_3wSvwDyYHSq</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype></control><display><type>article</type><title>IS200/IS605 family single-strand transposition: mechanism of IS608 strand transfer</title><source>MEDLINE</source><source>DOAJ Directory of Open Access Journals</source><source>Oxford Journals Open Access Collection</source><source>PubMed Central</source><source>Free Full-Text Journals in Chemistry</source><creator>He, Susu ; Guynet, Catherine ; Siguier, Patricia ; Hickman, Alison B ; Dyda, Fred ; Chandler, Mick ; Ton-Hoang, Bao</creator><creatorcontrib>He, Susu ; Guynet, Catherine ; Siguier, Patricia ; Hickman, Alison B ; Dyda, Fred ; Chandler, Mick ; Ton-Hoang, Bao</creatorcontrib><description>Transposase, TnpA, of the IS200/IS605 family member IS608, catalyses single-strand DNA transposition and is dimeric with hybrid catalytic sites composed of an HUH motif from one monomer and a catalytic Y127 present in an α-helix (αD) from the other (trans configuration). αD is attached to the main body by a flexible loop. Although the reactions leading to excision of a transposition intermediate are well characterized, little is known about the dynamic behaviour of the transpososome that drives this process. We provide evidence strongly supporting a strand transfer model involving rotation of both αD helices from the trans to the cis configuration (HUH and Y residues from the same monomer). Studies with TnpA heterodimers suggest that TnpA cleaves DNA in the trans configuration, and that the catalytic tyrosines linked to the 5'-phosphates exchange positions to allow rejoining of the cleaved strands (strand transfer) in the cis configuration. They further imply that, after excision of the transposon junction, TnpA should be reset to a trans configuration before the cleavage required for integration. Analysis also suggests that this mechanism is conserved among members of the IS200/IS605 family.</description><identifier>ISSN: 0305-1048</identifier><identifier>EISSN: 1362-4962</identifier><identifier>DOI: 10.1093/nar/gkt014</identifier><identifier>PMID: 23345619</identifier><language>eng</language><publisher>England: Oxford University Press</publisher><subject>Amino Acid Sequence ; Amino Acid Substitution ; Bacterial Proteins - chemistry ; Bacterial Proteins - genetics ; Bacterial Proteins - metabolism ; Base Sequence ; Biochemistry, Molecular Biology ; Catalytic Domain ; Consensus Sequence ; DNA Cleavage ; DNA Transposable Elements ; DNA, Bacterial - genetics ; Electrophoretic Mobility Shift Assay ; Escherichia coli ; Helicobacter pylori - enzymology ; Helicobacter pylori - genetics ; Inverted Repeat Sequences ; Life Sciences ; Molecular biology ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Nucleic Acid Enzymes ; Plasmids - genetics ; Transposases - chemistry ; Transposases - genetics ; Transposases - metabolism</subject><ispartof>Nucleic acids research, 2013-03, Vol.41 (5), p.3302-3313</ispartof><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><rights>The Author(s) 2013. Published by Oxford University Press. 2013</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><orcidid>0000-0003-1620-6495 ; 0000-0002-0292-6662 ; 0000-0003-1970-3411 ; 0000-0002-1785-6134</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3597680/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3597680/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,864,885,27923,27924,53790,53792</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23345619$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-00946739$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>He, Susu</creatorcontrib><creatorcontrib>Guynet, Catherine</creatorcontrib><creatorcontrib>Siguier, Patricia</creatorcontrib><creatorcontrib>Hickman, Alison B</creatorcontrib><creatorcontrib>Dyda, Fred</creatorcontrib><creatorcontrib>Chandler, Mick</creatorcontrib><creatorcontrib>Ton-Hoang, Bao</creatorcontrib><title>IS200/IS605 family single-strand transposition: mechanism of IS608 strand transfer</title><title>Nucleic acids research</title><addtitle>Nucleic Acids Res</addtitle><description>Transposase, TnpA, of the IS200/IS605 family member IS608, catalyses single-strand DNA transposition and is dimeric with hybrid catalytic sites composed of an HUH motif from one monomer and a catalytic Y127 present in an α-helix (αD) from the other (trans configuration). αD is attached to the main body by a flexible loop. Although the reactions leading to excision of a transposition intermediate are well characterized, little is known about the dynamic behaviour of the transpososome that drives this process. We provide evidence strongly supporting a strand transfer model involving rotation of both αD helices from the trans to the cis configuration (HUH and Y residues from the same monomer). Studies with TnpA heterodimers suggest that TnpA cleaves DNA in the trans configuration, and that the catalytic tyrosines linked to the 5'-phosphates exchange positions to allow rejoining of the cleaved strands (strand transfer) in the cis configuration. They further imply that, after excision of the transposon junction, TnpA should be reset to a trans configuration before the cleavage required for integration. Analysis also suggests that this mechanism is conserved among members of the IS200/IS605 family.</description><subject>Amino Acid Sequence</subject><subject>Amino Acid Substitution</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - metabolism</subject><subject>Base Sequence</subject><subject>Biochemistry, Molecular Biology</subject><subject>Catalytic Domain</subject><subject>Consensus Sequence</subject><subject>DNA Cleavage</subject><subject>DNA Transposable Elements</subject><subject>DNA, Bacterial - genetics</subject><subject>Electrophoretic Mobility Shift Assay</subject><subject>Escherichia coli</subject><subject>Helicobacter pylori - enzymology</subject><subject>Helicobacter pylori - genetics</subject><subject>Inverted Repeat Sequences</subject><subject>Life Sciences</subject><subject>Molecular biology</subject><subject>Molecular Sequence Data</subject><subject>Mutagenesis, Site-Directed</subject><subject>Nucleic Acid Enzymes</subject><subject>Plasmids - genetics</subject><subject>Transposases - chemistry</subject><subject>Transposases - genetics</subject><subject>Transposases - metabolism</subject><issn>0305-1048</issn><issn>1362-4962</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkE9Lw0AQxRdRbK1e_ACyVw-xszub3awHoRS1hYJg9Rw2yaZZzZ-STQv99qZUpXqZgZnfe_MYQq4Z3DHQOK5NO159dsDECRkylDwQWvJTMgSEMGAgogG58P4DeoKF4pwMOKIIJdND8jpfcoDxfCkhpLmpXLmj3tWr0ga-a02d0X3168a7zjX1Pa1sWpja-Yo2Od3LInoM5ra9JGe5Kb29-u4j8v70-DadBYuX5_l0sggKBOgCFVrNU5NlNsoxUanlgqVoUYgoAy1MgtIYzhOmjA4tByVTZhmwnGuNWhkckYeD73qTVDZLbd0nKON16yrT7uLGuPjvpnZFvGq2MYZayQh6g9uDQfFPNpss4v0M-hxSod6ynr05PvaL_3wSvwDyYHSq</recordid><startdate>20130301</startdate><enddate>20130301</enddate><creator>He, Susu</creator><creator>Guynet, Catherine</creator><creator>Siguier, Patricia</creator><creator>Hickman, Alison B</creator><creator>Dyda, Fred</creator><creator>Chandler, Mick</creator><creator>Ton-Hoang, Bao</creator><general>Oxford University Press</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>1XC</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0003-1620-6495</orcidid><orcidid>https://orcid.org/0000-0002-0292-6662</orcidid><orcidid>https://orcid.org/0000-0003-1970-3411</orcidid><orcidid>https://orcid.org/0000-0002-1785-6134</orcidid></search><sort><creationdate>20130301</creationdate><title>IS200/IS605 family single-strand transposition: mechanism of IS608 strand transfer</title><author>He, Susu ; Guynet, Catherine ; Siguier, Patricia ; Hickman, Alison B ; Dyda, Fred ; Chandler, Mick ; Ton-Hoang, Bao</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-h300t-75e92cadde8f3b7ce241c3e3448d094ab36aa22b17a95e2076c1e101f299397a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Amino Acid Sequence</topic><topic>Amino Acid Substitution</topic><topic>Bacterial Proteins - chemistry</topic><topic>Bacterial Proteins - genetics</topic><topic>Bacterial Proteins - metabolism</topic><topic>Base Sequence</topic><topic>Biochemistry, Molecular Biology</topic><topic>Catalytic Domain</topic><topic>Consensus Sequence</topic><topic>DNA Cleavage</topic><topic>DNA Transposable Elements</topic><topic>DNA, Bacterial - genetics</topic><topic>Electrophoretic Mobility Shift Assay</topic><topic>Escherichia coli</topic><topic>Helicobacter pylori - enzymology</topic><topic>Helicobacter pylori - genetics</topic><topic>Inverted Repeat Sequences</topic><topic>Life Sciences</topic><topic>Molecular biology</topic><topic>Molecular Sequence Data</topic><topic>Mutagenesis, Site-Directed</topic><topic>Nucleic Acid Enzymes</topic><topic>Plasmids - genetics</topic><topic>Transposases - chemistry</topic><topic>Transposases - genetics</topic><topic>Transposases - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>He, Susu</creatorcontrib><creatorcontrib>Guynet, Catherine</creatorcontrib><creatorcontrib>Siguier, Patricia</creatorcontrib><creatorcontrib>Hickman, Alison B</creatorcontrib><creatorcontrib>Dyda, Fred</creatorcontrib><creatorcontrib>Chandler, Mick</creatorcontrib><creatorcontrib>Ton-Hoang, Bao</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>Hyper Article en Ligne (HAL)</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Nucleic acids research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>He, Susu</au><au>Guynet, Catherine</au><au>Siguier, Patricia</au><au>Hickman, Alison B</au><au>Dyda, Fred</au><au>Chandler, Mick</au><au>Ton-Hoang, Bao</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>IS200/IS605 family single-strand transposition: mechanism of IS608 strand transfer</atitle><jtitle>Nucleic acids research</jtitle><addtitle>Nucleic Acids Res</addtitle><date>2013-03-01</date><risdate>2013</risdate><volume>41</volume><issue>5</issue><spage>3302</spage><epage>3313</epage><pages>3302-3313</pages><issn>0305-1048</issn><eissn>1362-4962</eissn><abstract>Transposase, TnpA, of the IS200/IS605 family member IS608, catalyses single-strand DNA transposition and is dimeric with hybrid catalytic sites composed of an HUH motif from one monomer and a catalytic Y127 present in an α-helix (αD) from the other (trans configuration). αD is attached to the main body by a flexible loop. Although the reactions leading to excision of a transposition intermediate are well characterized, little is known about the dynamic behaviour of the transpososome that drives this process. We provide evidence strongly supporting a strand transfer model involving rotation of both αD helices from the trans to the cis configuration (HUH and Y residues from the same monomer). Studies with TnpA heterodimers suggest that TnpA cleaves DNA in the trans configuration, and that the catalytic tyrosines linked to the 5'-phosphates exchange positions to allow rejoining of the cleaved strands (strand transfer) in the cis configuration. They further imply that, after excision of the transposon junction, TnpA should be reset to a trans configuration before the cleavage required for integration. Analysis also suggests that this mechanism is conserved among members of the IS200/IS605 family.</abstract><cop>England</cop><pub>Oxford University Press</pub><pmid>23345619</pmid><doi>10.1093/nar/gkt014</doi><tpages>12</tpages><orcidid>https://orcid.org/0000-0003-1620-6495</orcidid><orcidid>https://orcid.org/0000-0002-0292-6662</orcidid><orcidid>https://orcid.org/0000-0003-1970-3411</orcidid><orcidid>https://orcid.org/0000-0002-1785-6134</orcidid><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0305-1048 |
| ispartof | Nucleic acids research, 2013-03, Vol.41 (5), p.3302-3313 |
| issn | 0305-1048 1362-4962 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3597680 |
| source | MEDLINE; DOAJ Directory of Open Access Journals; Oxford Journals Open Access Collection; PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | Amino Acid Sequence Amino Acid Substitution Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism Base Sequence Biochemistry, Molecular Biology Catalytic Domain Consensus Sequence DNA Cleavage DNA Transposable Elements DNA, Bacterial - genetics Electrophoretic Mobility Shift Assay Escherichia coli Helicobacter pylori - enzymology Helicobacter pylori - genetics Inverted Repeat Sequences Life Sciences Molecular biology Molecular Sequence Data Mutagenesis, Site-Directed Nucleic Acid Enzymes Plasmids - genetics Transposases - chemistry Transposases - genetics Transposases - metabolism |
| title | IS200/IS605 family single-strand transposition: mechanism of IS608 strand transfer |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-12T10%3A16%3A10IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-pubmed_hal_p&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=IS200/IS605%20family%20single-strand%20transposition:%20mechanism%20of%20IS608%20strand%20transfer&rft.jtitle=Nucleic%20acids%20research&rft.au=He,%20Susu&rft.date=2013-03-01&rft.volume=41&rft.issue=5&rft.spage=3302&rft.epage=3313&rft.pages=3302-3313&rft.issn=0305-1048&rft.eissn=1362-4962&rft_id=info:doi/10.1093/nar/gkt014&rft_dat=%3Cpubmed_hal_p%3E23345619%3C/pubmed_hal_p%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_id=info:pmid/23345619&rfr_iscdi=true |