Tightening the Belt on Polymerases: Evaluating the Physical Constraints on Enzyme Substrate Size

To test the limits of polymerase enzyme activity on geometrically constrained DNAs, four very small synthetic circular DNAs were constructed by using newly developed methods. Surprisingly, even a 13‐nucleotide circular DNA (1) can be copied successfully by both DNA and RNA polymerases, despite the v...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Angewandte Chemie International Edition 1999-12, Vol.38 (24), p.3654-3657
Hauptverfasser: Frieden, Miriam, Pedroso, Enrique, Kool, Eric T.
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 3657
container_issue 24
container_start_page 3654
container_title Angewandte Chemie International Edition
container_volume 38
creator Frieden, Miriam
Pedroso, Enrique
Kool, Eric T.
description To test the limits of polymerase enzyme activity on geometrically constrained DNAs, four very small synthetic circular DNAs were constructed by using newly developed methods. Surprisingly, even a 13‐nucleotide circular DNA (1) can be copied successfully by both DNA and RNA polymerases, despite the very small diameter and large degree of distortion in this synthetic DNA. The picture shows models to indicate the relative sizes of 1 and the Klenow fragment of the DNA polymerase I from E. coli.
doi_str_mv 10.1002/(SICI)1521-3773(19991216)38:24<3654::AID-ANIE3654>3.0.CO;2-S
format Article
fullrecord <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_proquest_miscellaneous_1859311858</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>1859311858</sourcerecordid><originalsourceid>FETCH-LOGICAL-p1454-c56787354a8a73a4e1dd0c2512b700ab3828b575d24b51b9b040457d709d89fd3</originalsourceid><addsrcrecordid>eNpNkV1PwjAUhhujEb_-gtklXgz7uXZoTHCgLiFCAl4fO1ZgZmy4bhr89XZRjDftOafve5K-D0JDgnsEY3rdncVRfEUEJT6TknVJGIaEkuCKqT7ltywQvN8fxEN_8ByP2u6O9XAvmtxQf3aATv6Mh67mjPlSCdJBp9a-ue1K4eAYdQgOeMgIO0Gv82y1rk2RFSuvXhvv3uS1VxbetMx3G1Npa2zfG33ovNH1XjNd72y20LkXlYWtK50VtW09o-LLebxZk7TT2lXZlzlHR0udW3Pxe5-hl4fRPHryx5PHOBqM_S3hgvsLEUglmeBaack0NyRN8YIKQhOJsU6YoioRUqSUJ4IkYYI55kKmEoepCpcpO0Pdn73bqnxvjK1hk9mFyXNdmLKxQJRwP3anctLLX2mTbEwK2yrb6GoH-1Sc4PVH8JnlZvfvHVpC0AKCNmdoc4Y9IGAKKIcWCTg-sOcDDDBEE3DGvxn7BvnLiQM</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1859311858</pqid></control><display><type>article</type><title>Tightening the Belt on Polymerases: Evaluating the Physical Constraints on Enzyme Substrate Size</title><source>Wiley Journals</source><creator>Frieden, Miriam ; Pedroso, Enrique ; Kool, Eric T.</creator><creatorcontrib>Frieden, Miriam ; Pedroso, Enrique ; Kool, Eric T.</creatorcontrib><description>To test the limits of polymerase enzyme activity on geometrically constrained DNAs, four very small synthetic circular DNAs were constructed by using newly developed methods. Surprisingly, even a 13‐nucleotide circular DNA (1) can be copied successfully by both DNA and RNA polymerases, despite the very small diameter and large degree of distortion in this synthetic DNA. The picture shows models to indicate the relative sizes of 1 and the Klenow fragment of the DNA polymerase I from E. coli.</description><identifier>ISSN: 1433-7851</identifier><identifier>EISSN: 1521-3773</identifier><identifier>DOI: 10.1002/(SICI)1521-3773(19991216)38:24&lt;3654::AID-ANIE3654&gt;3.0.CO;2-S</identifier><identifier>PMID: 10649313</identifier><language>eng</language><publisher>Weinheim: WILEY‐VCH Verlag GmbH</publisher><subject>DNA recognition ; Polymerases ; RNA ; Transcription</subject><ispartof>Angewandte Chemie International Edition, 1999-12, Vol.38 (24), p.3654-3657</ispartof><rights>1999 WILEY‐VCH Verlag GmbH, Weinheim, Fed. Rep. of Germany</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2F%28SICI%291521-3773%2819991216%2938%3A24%3C3654%3A%3AAID-ANIE3654%3E3.0.CO%3B2-S$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2F%28SICI%291521-3773%2819991216%2938%3A24%3C3654%3A%3AAID-ANIE3654%3E3.0.CO%3B2-S$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,27924,27925,45574,45575</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10649313$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Frieden, Miriam</creatorcontrib><creatorcontrib>Pedroso, Enrique</creatorcontrib><creatorcontrib>Kool, Eric T.</creatorcontrib><title>Tightening the Belt on Polymerases: Evaluating the Physical Constraints on Enzyme Substrate Size</title><title>Angewandte Chemie International Edition</title><addtitle>Angew Chem Int Ed Engl</addtitle><description>To test the limits of polymerase enzyme activity on geometrically constrained DNAs, four very small synthetic circular DNAs were constructed by using newly developed methods. Surprisingly, even a 13‐nucleotide circular DNA (1) can be copied successfully by both DNA and RNA polymerases, despite the very small diameter and large degree of distortion in this synthetic DNA. The picture shows models to indicate the relative sizes of 1 and the Klenow fragment of the DNA polymerase I from E. coli.</description><subject>DNA recognition</subject><subject>Polymerases</subject><subject>RNA</subject><subject>Transcription</subject><issn>1433-7851</issn><issn>1521-3773</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><recordid>eNpNkV1PwjAUhhujEb_-gtklXgz7uXZoTHCgLiFCAl4fO1ZgZmy4bhr89XZRjDftOafve5K-D0JDgnsEY3rdncVRfEUEJT6TknVJGIaEkuCKqT7ltywQvN8fxEN_8ByP2u6O9XAvmtxQf3aATv6Mh67mjPlSCdJBp9a-ue1K4eAYdQgOeMgIO0Gv82y1rk2RFSuvXhvv3uS1VxbetMx3G1Npa2zfG33ovNH1XjNd72y20LkXlYWtK50VtW09o-LLebxZk7TT2lXZlzlHR0udW3Pxe5-hl4fRPHryx5PHOBqM_S3hgvsLEUglmeBaack0NyRN8YIKQhOJsU6YoioRUqSUJ4IkYYI55kKmEoepCpcpO0Pdn73bqnxvjK1hk9mFyXNdmLKxQJRwP3anctLLX2mTbEwK2yrb6GoH-1Sc4PVH8JnlZvfvHVpC0AKCNmdoc4Y9IGAKKIcWCTg-sOcDDDBEE3DGvxn7BvnLiQM</recordid><startdate>19991216</startdate><enddate>19991216</enddate><creator>Frieden, Miriam</creator><creator>Pedroso, Enrique</creator><creator>Kool, Eric T.</creator><general>WILEY‐VCH Verlag GmbH</general><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>19991216</creationdate><title>Tightening the Belt on Polymerases: Evaluating the Physical Constraints on Enzyme Substrate Size</title><author>Frieden, Miriam ; Pedroso, Enrique ; Kool, Eric T.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p1454-c56787354a8a73a4e1dd0c2512b700ab3828b575d24b51b9b040457d709d89fd3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>DNA recognition</topic><topic>Polymerases</topic><topic>RNA</topic><topic>Transcription</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Frieden, Miriam</creatorcontrib><creatorcontrib>Pedroso, Enrique</creatorcontrib><creatorcontrib>Kool, Eric T.</creatorcontrib><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>Angewandte Chemie International Edition</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Frieden, Miriam</au><au>Pedroso, Enrique</au><au>Kool, Eric T.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Tightening the Belt on Polymerases: Evaluating the Physical Constraints on Enzyme Substrate Size</atitle><jtitle>Angewandte Chemie International Edition</jtitle><addtitle>Angew Chem Int Ed Engl</addtitle><date>1999-12-16</date><risdate>1999</risdate><volume>38</volume><issue>24</issue><spage>3654</spage><epage>3657</epage><pages>3654-3657</pages><issn>1433-7851</issn><eissn>1521-3773</eissn><abstract>To test the limits of polymerase enzyme activity on geometrically constrained DNAs, four very small synthetic circular DNAs were constructed by using newly developed methods. Surprisingly, even a 13‐nucleotide circular DNA (1) can be copied successfully by both DNA and RNA polymerases, despite the very small diameter and large degree of distortion in this synthetic DNA. The picture shows models to indicate the relative sizes of 1 and the Klenow fragment of the DNA polymerase I from E. coli.</abstract><cop>Weinheim</cop><pub>WILEY‐VCH Verlag GmbH</pub><pmid>10649313</pmid><doi>10.1002/(SICI)1521-3773(19991216)38:24&lt;3654::AID-ANIE3654&gt;3.0.CO;2-S</doi><tpages>4</tpages></addata></record>
fulltext fulltext
identifier ISSN: 1433-7851
ispartof Angewandte Chemie International Edition, 1999-12, Vol.38 (24), p.3654-3657
issn 1433-7851
1521-3773
language eng
recordid cdi_proquest_miscellaneous_1859311858
source Wiley Journals
subjects DNA recognition
Polymerases
RNA
Transcription
title Tightening the Belt on Polymerases: Evaluating the Physical Constraints on Enzyme Substrate Size
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-28T12%3A47%3A20IST&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=Tightening%20the%20Belt%20on%20Polymerases:%20Evaluating%20the%20Physical%20Constraints%20on%20Enzyme%20Substrate%20Size&rft.jtitle=Angewandte%20Chemie%20International%20Edition&rft.au=Frieden,%20Miriam&rft.date=1999-12-16&rft.volume=38&rft.issue=24&rft.spage=3654&rft.epage=3657&rft.pages=3654-3657&rft.issn=1433-7851&rft.eissn=1521-3773&rft_id=info:doi/10.1002/(SICI)1521-3773(19991216)38:24%3C3654::AID-ANIE3654%3E3.0.CO;2-S&rft_dat=%3Cproquest_pubme%3E1859311858%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=1859311858&rft_id=info:pmid/10649313&rfr_iscdi=true