Crystallization and preliminary X-ray characterization of the eukaryotic replication terminator Reb1-Ter DNA complex
The Reb1 protein from Schizosaccharomyces pombe is a member of a family of proteins that control programmed replication termination and/or transcription termination in eukaryotic cells. These events occur at naturally occurring replication fork barriers (RFBs), where Reb1 binds to termination (Ter)...
Gespeichert in:
| Veröffentlicht in: | Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2015-04, Vol.71 (4), p.414-418 |
|---|---|
| Hauptverfasser: | , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 418 |
|---|---|
| container_issue | 4 |
| container_start_page | 414 |
| container_title | Acta crystallographica. Section F, Structural biology and crystallization communications |
| container_volume | 71 |
| creator | Jaiswal, Rahul Singh, Samarendra K. Bastia, Deepak Escalante, Carlos R. |
| description | The Reb1 protein from Schizosaccharomyces pombe is a member of a family of proteins that control programmed replication termination and/or transcription termination in eukaryotic cells. These events occur at naturally occurring replication fork barriers (RFBs), where Reb1 binds to termination (Ter) DNA sites and coordinates the polar arrest of replication forks and transcription approaching in opposite directions. The Reb1 DNA‐binding and replication‐termination domain was expressed in Escherichia coli, purified and crystallized in complex with a 26‐mer DNA Ter site. Batch crystallization under oil was required to produce crystals of good quality for data collection. Crystals grew in space group P21, with unit‐cell parameters a = 68.9, b = 162.9, c = 71.1 Å, β = 94.7°. The crystals diffracted to a resolution of 3.0 Å. The crystals were mosaic and required two or three cycles of annealing. This study is the first to yield structural information about this important family of proteins and will provide insights into the mechanism of replication and transcription termination. |
| doi_str_mv | 10.1107/S2053230X15004112 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4388176</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>3646928161</sourcerecordid><originalsourceid>FETCH-LOGICAL-c5422-23d7a38355b2d9d08f90b4d452677b5a54a58fa659ab077655498344cafe1b0e3</originalsourceid><addsrcrecordid>eNqFkcFu1DAQhiMEolXpA3BBEVy4BGzHjpML0mrLtohVkbZFlJPlOBPWrRMH24EuT4-jtKsCB062PN_3e-xJkucYvcEY8bcXBLGc5OgKM4QoxuRRcjgdZdPZ4wf7g-TY-2uE0KRhXj1NDggracUQOUzC0u18kMboXzJo26eyb9LBgdGd7qXbpVeZk7tUbaWTKoC7x2ybhi2kMN5EyAatUgeD0WquRnDSg3XpBmqcXYJLT84XqbLdYOD2WfKklcbD8d16lHxevb9cnmXrT6cflot1phglJDbfcJmXOWM1aaoGlW2FatpQRgrOayYZlaxsZcEqWSPOC8ZoVeaUKtkCrhHkR8m7OXcY6w4aBX1w0ojB6S52LazU4s9Kr7fim_0haF6WmBcx4OUcYH3QwisdQG2V7XtQQWBCyqriEXp9d4uz30fwQXTaKzBG9mBHL3DBCSo5oSyir_5Cr-3o-vgHE4UIJpzjSOGZUs5676Ddd4yRmIYo_pl9dF48fOreuJ90BKoZ-KkN7P6fKBZfV2SzZqia3Gx2tQ9wu3eluxEFzzkTX85PxRqji83q45k4yX8D0XLJuQ</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1670212771</pqid></control><display><type>article</type><title>Crystallization and preliminary X-ray characterization of the eukaryotic replication terminator Reb1-Ter DNA complex</title><source>MEDLINE</source><source>Access via Wiley Online Library</source><source>PubMed Central</source><source>Free Full-Text Journals in Chemistry</source><creator>Jaiswal, Rahul ; Singh, Samarendra K. ; Bastia, Deepak ; Escalante, Carlos R.</creator><creatorcontrib>Jaiswal, Rahul ; Singh, Samarendra K. ; Bastia, Deepak ; Escalante, Carlos R. ; Brookhaven National Laboratory (BNL), Upton, NY (United States)</creatorcontrib><description>The Reb1 protein from Schizosaccharomyces pombe is a member of a family of proteins that control programmed replication termination and/or transcription termination in eukaryotic cells. These events occur at naturally occurring replication fork barriers (RFBs), where Reb1 binds to termination (Ter) DNA sites and coordinates the polar arrest of replication forks and transcription approaching in opposite directions. The Reb1 DNA‐binding and replication‐termination domain was expressed in Escherichia coli, purified and crystallized in complex with a 26‐mer DNA Ter site. Batch crystallization under oil was required to produce crystals of good quality for data collection. Crystals grew in space group P21, with unit‐cell parameters a = 68.9, b = 162.9, c = 71.1 Å, β = 94.7°. The crystals diffracted to a resolution of 3.0 Å. The crystals were mosaic and required two or three cycles of annealing. This study is the first to yield structural information about this important family of proteins and will provide insights into the mechanism of replication and transcription termination.</description><identifier>ISSN: 2053-230X</identifier><identifier>ISSN: 1744-3091</identifier><identifier>EISSN: 2053-230X</identifier><identifier>EISSN: 1744-3091</identifier><identifier>DOI: 10.1107/S2053230X15004112</identifier><identifier>PMID: 25849502</identifier><language>eng</language><publisher>5 Abbey Square, Chester, Cheshire CH1 2HU, England: International Union of Crystallography</publisher><subject>Amino Acid Sequence ; Crystallization ; Crystallography, X-Ray ; DNA Replication - physiology ; DNA-Binding Proteins - chemistry ; DNA-Binding Proteins - genetics ; eukaryotic ; Molecular Sequence Data ; protein-DNA complex ; Reb1 ; Research Communications ; RNA Pol I ; Schizosaccharomyces - genetics ; Schizosaccharomyces pombe Proteins - chemistry ; Schizosaccharomyces pombe Proteins - genetics ; Transcription Factors - chemistry ; Transcription Factors - genetics ; transcription termination ; Transcription Termination, Genetic - physiology</subject><ispartof>Acta crystallographica. Section F, Structural biology and crystallization communications, 2015-04, Vol.71 (4), p.414-418</ispartof><rights>International Union of Crystallography, 2015</rights><rights>International Union of Crystallography 2015 2015</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5422-23d7a38355b2d9d08f90b4d452677b5a54a58fa659ab077655498344cafe1b0e3</citedby><cites>FETCH-LOGICAL-c5422-23d7a38355b2d9d08f90b4d452677b5a54a58fa659ab077655498344cafe1b0e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4388176/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4388176/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,1417,27924,27925,45574,45575,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/25849502$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/1228997$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Jaiswal, Rahul</creatorcontrib><creatorcontrib>Singh, Samarendra K.</creatorcontrib><creatorcontrib>Bastia, Deepak</creatorcontrib><creatorcontrib>Escalante, Carlos R.</creatorcontrib><creatorcontrib>Brookhaven National Laboratory (BNL), Upton, NY (United States)</creatorcontrib><title>Crystallization and preliminary X-ray characterization of the eukaryotic replication terminator Reb1-Ter DNA complex</title><title>Acta crystallographica. Section F, Structural biology and crystallization communications</title><addtitle>Acta Crystallographica Section F</addtitle><description>The Reb1 protein from Schizosaccharomyces pombe is a member of a family of proteins that control programmed replication termination and/or transcription termination in eukaryotic cells. These events occur at naturally occurring replication fork barriers (RFBs), where Reb1 binds to termination (Ter) DNA sites and coordinates the polar arrest of replication forks and transcription approaching in opposite directions. The Reb1 DNA‐binding and replication‐termination domain was expressed in Escherichia coli, purified and crystallized in complex with a 26‐mer DNA Ter site. Batch crystallization under oil was required to produce crystals of good quality for data collection. Crystals grew in space group P21, with unit‐cell parameters a = 68.9, b = 162.9, c = 71.1 Å, β = 94.7°. The crystals diffracted to a resolution of 3.0 Å. The crystals were mosaic and required two or three cycles of annealing. This study is the first to yield structural information about this important family of proteins and will provide insights into the mechanism of replication and transcription termination.</description><subject>Amino Acid Sequence</subject><subject>Crystallization</subject><subject>Crystallography, X-Ray</subject><subject>DNA Replication - physiology</subject><subject>DNA-Binding Proteins - chemistry</subject><subject>DNA-Binding Proteins - genetics</subject><subject>eukaryotic</subject><subject>Molecular Sequence Data</subject><subject>protein-DNA complex</subject><subject>Reb1</subject><subject>Research Communications</subject><subject>RNA Pol I</subject><subject>Schizosaccharomyces - genetics</subject><subject>Schizosaccharomyces pombe Proteins - chemistry</subject><subject>Schizosaccharomyces pombe Proteins - genetics</subject><subject>Transcription Factors - chemistry</subject><subject>Transcription Factors - genetics</subject><subject>transcription termination</subject><subject>Transcription Termination, Genetic - physiology</subject><issn>2053-230X</issn><issn>1744-3091</issn><issn>2053-230X</issn><issn>1744-3091</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkcFu1DAQhiMEolXpA3BBEVy4BGzHjpML0mrLtohVkbZFlJPlOBPWrRMH24EuT4-jtKsCB062PN_3e-xJkucYvcEY8bcXBLGc5OgKM4QoxuRRcjgdZdPZ4wf7g-TY-2uE0KRhXj1NDggracUQOUzC0u18kMboXzJo26eyb9LBgdGd7qXbpVeZk7tUbaWTKoC7x2ybhi2kMN5EyAatUgeD0WquRnDSg3XpBmqcXYJLT84XqbLdYOD2WfKklcbD8d16lHxevb9cnmXrT6cflot1phglJDbfcJmXOWM1aaoGlW2FatpQRgrOayYZlaxsZcEqWSPOC8ZoVeaUKtkCrhHkR8m7OXcY6w4aBX1w0ojB6S52LazU4s9Kr7fim_0haF6WmBcx4OUcYH3QwisdQG2V7XtQQWBCyqriEXp9d4uz30fwQXTaKzBG9mBHL3DBCSo5oSyir_5Cr-3o-vgHE4UIJpzjSOGZUs5676Ddd4yRmIYo_pl9dF48fOreuJ90BKoZ-KkN7P6fKBZfV2SzZqia3Gx2tQ9wu3eluxEFzzkTX85PxRqji83q45k4yX8D0XLJuQ</recordid><startdate>201504</startdate><enddate>201504</enddate><creator>Jaiswal, Rahul</creator><creator>Singh, Samarendra K.</creator><creator>Bastia, Deepak</creator><creator>Escalante, Carlos R.</creator><general>International Union of Crystallography</general><general>Wiley Subscription Services, Inc</general><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7T7</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>7X8</scope><scope>OTOTI</scope><scope>5PM</scope></search><sort><creationdate>201504</creationdate><title>Crystallization and preliminary X-ray characterization of the eukaryotic replication terminator Reb1-Ter DNA complex</title><author>Jaiswal, Rahul ; Singh, Samarendra K. ; Bastia, Deepak ; Escalante, Carlos R.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5422-23d7a38355b2d9d08f90b4d452677b5a54a58fa659ab077655498344cafe1b0e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><topic>Amino Acid Sequence</topic><topic>Crystallization</topic><topic>Crystallography, X-Ray</topic><topic>DNA Replication - physiology</topic><topic>DNA-Binding Proteins - chemistry</topic><topic>DNA-Binding Proteins - genetics</topic><topic>eukaryotic</topic><topic>Molecular Sequence Data</topic><topic>protein-DNA complex</topic><topic>Reb1</topic><topic>Research Communications</topic><topic>RNA Pol I</topic><topic>Schizosaccharomyces - genetics</topic><topic>Schizosaccharomyces pombe Proteins - chemistry</topic><topic>Schizosaccharomyces pombe Proteins - genetics</topic><topic>Transcription Factors - chemistry</topic><topic>Transcription Factors - genetics</topic><topic>transcription termination</topic><topic>Transcription Termination, Genetic - physiology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Jaiswal, Rahul</creatorcontrib><creatorcontrib>Singh, Samarendra K.</creatorcontrib><creatorcontrib>Bastia, Deepak</creatorcontrib><creatorcontrib>Escalante, Carlos R.</creatorcontrib><creatorcontrib>Brookhaven National Laboratory (BNL), Upton, NY (United States)</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><collection>OSTI.GOV</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Acta crystallographica. Section F, Structural biology and crystallization communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Jaiswal, Rahul</au><au>Singh, Samarendra K.</au><au>Bastia, Deepak</au><au>Escalante, Carlos R.</au><aucorp>Brookhaven National Laboratory (BNL), Upton, NY (United States)</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystallization and preliminary X-ray characterization of the eukaryotic replication terminator Reb1-Ter DNA complex</atitle><jtitle>Acta crystallographica. Section F, Structural biology and crystallization communications</jtitle><addtitle>Acta Crystallographica Section F</addtitle><date>2015-04</date><risdate>2015</risdate><volume>71</volume><issue>4</issue><spage>414</spage><epage>418</epage><pages>414-418</pages><issn>2053-230X</issn><issn>1744-3091</issn><eissn>2053-230X</eissn><eissn>1744-3091</eissn><abstract>The Reb1 protein from Schizosaccharomyces pombe is a member of a family of proteins that control programmed replication termination and/or transcription termination in eukaryotic cells. These events occur at naturally occurring replication fork barriers (RFBs), where Reb1 binds to termination (Ter) DNA sites and coordinates the polar arrest of replication forks and transcription approaching in opposite directions. The Reb1 DNA‐binding and replication‐termination domain was expressed in Escherichia coli, purified and crystallized in complex with a 26‐mer DNA Ter site. Batch crystallization under oil was required to produce crystals of good quality for data collection. Crystals grew in space group P21, with unit‐cell parameters a = 68.9, b = 162.9, c = 71.1 Å, β = 94.7°. The crystals diffracted to a resolution of 3.0 Å. The crystals were mosaic and required two or three cycles of annealing. This study is the first to yield structural information about this important family of proteins and will provide insights into the mechanism of replication and transcription termination.</abstract><cop>5 Abbey Square, Chester, Cheshire CH1 2HU, England</cop><pub>International Union of Crystallography</pub><pmid>25849502</pmid><doi>10.1107/S2053230X15004112</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 2053-230X |
| ispartof | Acta crystallographica. Section F, Structural biology and crystallization communications, 2015-04, Vol.71 (4), p.414-418 |
| issn | 2053-230X 1744-3091 2053-230X 1744-3091 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4388176 |
| source | MEDLINE; Access via Wiley Online Library; PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | Amino Acid Sequence Crystallization Crystallography, X-Ray DNA Replication - physiology DNA-Binding Proteins - chemistry DNA-Binding Proteins - genetics eukaryotic Molecular Sequence Data protein-DNA complex Reb1 Research Communications RNA Pol I Schizosaccharomyces - genetics Schizosaccharomyces pombe Proteins - chemistry Schizosaccharomyces pombe Proteins - genetics Transcription Factors - chemistry Transcription Factors - genetics transcription termination Transcription Termination, Genetic - physiology |
| title | Crystallization and preliminary X-ray characterization of the eukaryotic replication terminator Reb1-Ter DNA complex |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-27T00%3A05%3A11IST&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=Crystallization%20and%20preliminary%20X-ray%20characterization%20of%20the%20eukaryotic%20replication%20terminator%20Reb1-Ter%20DNA%20complex&rft.jtitle=Acta%20crystallographica.%20Section%20F,%20Structural%20biology%20and%20crystallization%20communications&rft.au=Jaiswal,%20Rahul&rft.aucorp=Brookhaven%20National%20Laboratory%20(BNL),%20Upton,%20NY%20(United%20States)&rft.date=2015-04&rft.volume=71&rft.issue=4&rft.spage=414&rft.epage=418&rft.pages=414-418&rft.issn=2053-230X&rft.eissn=2053-230X&rft_id=info:doi/10.1107/S2053230X15004112&rft_dat=%3Cproquest_pubme%3E3646928161%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=1670212771&rft_id=info:pmid/25849502&rfr_iscdi=true |