Interaction of mithramycin with isolated GC and CG sites
We have studied the interaction of the GC‐specific, minor groove‐binding ligand, mithramycin, with cloned DNA inserts containing isolated GC and CG sites flanked by regions of (AT)n and An · Tn using DNase I and hydroxyl radical footprinting. We find that mithramycin binds to GC better than CG and t...
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| Veröffentlicht in: | Journal of molecular recognition 1994-09, Vol.7 (3), p.189-197 |
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| container_title | Journal of molecular recognition |
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| creator | Carpenter, Mark L. Cassidy, Sarah A. Fox, Keith R. |
| description | We have studied the interaction of the GC‐specific, minor groove‐binding ligand, mithramycin, with cloned DNA inserts containing isolated GC and CG sites flanked by regions of (AT)n and An · Tn using DNase I and hydroxyl radical footprinting. We find that mithramycin binds to GC better than CG and that AGCT is a better site than TGCA. Sites flanked by (AT)n appear to be bound better than those surrounded by An · Tn. Although no footprints are produced at T9GCA9 and T15CGA15, DNase I cleavage is enhanced with the GC sites suggesting that there is some interaction with the ligand. Mithramycin also alters the DNase I cleavage of (GA)n · (CT)n. |
| doi_str_mv | 10.1002/jmr.300070306 |
| format | Article |
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We find that mithramycin binds to GC better than CG and that AGCT is a better site than TGCA. Sites flanked by (AT)n appear to be bound better than those surrounded by An · Tn. Although no footprints are produced at T9GCA9 and T15CGA15, DNase I cleavage is enhanced with the GC sites suggesting that there is some interaction with the ligand. Mithramycin also alters the DNase I cleavage of (GA)n · (CT)n.</description><identifier>ISSN: 0952-3499</identifier><identifier>EISSN: 1099-1352</identifier><identifier>DOI: 10.1002/jmr.300070306</identifier><identifier>PMID: 7880543</identifier><language>eng</language><publisher>Chichester, UK: John Wiley & Sons, Ltd</publisher><subject>Adenine - chemistry ; Base Sequence ; Binding Sites ; Carbohydrate Sequence ; Cytosine - chemistry ; Deoxyribonuclease I ; DNA - chemistry ; DNase I footprinting ; Electrophoresis, Polyacrylamide Gel ; Guanine - chemistry ; Hydroxyl Radical ; Minor groove binding ; Mithramycin ; Molecular Sequence Data ; Molecular Structure ; Plicamycin - chemistry ; Sequence recognition ; Thymine - chemistry</subject><ispartof>Journal of molecular recognition, 1994-09, Vol.7 (3), p.189-197</ispartof><rights>Copyright © 1994 John Wiley & Sons Ltd.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c2896-d7d7a597d0dfec21beb0cd34947bd3110c83232b483c616942d361b5289f53603</citedby><cites>FETCH-LOGICAL-c2896-d7d7a597d0dfec21beb0cd34947bd3110c83232b483c616942d361b5289f53603</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fjmr.300070306$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fjmr.300070306$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27901,27902,45550,45551</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7880543$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Carpenter, Mark L.</creatorcontrib><creatorcontrib>Cassidy, Sarah A.</creatorcontrib><creatorcontrib>Fox, Keith R.</creatorcontrib><title>Interaction of mithramycin with isolated GC and CG sites</title><title>Journal of molecular recognition</title><addtitle>J. Mol. Recognit</addtitle><description>We have studied the interaction of the GC‐specific, minor groove‐binding ligand, mithramycin, with cloned DNA inserts containing isolated GC and CG sites flanked by regions of (AT)n and An · Tn using DNase I and hydroxyl radical footprinting. We find that mithramycin binds to GC better than CG and that AGCT is a better site than TGCA. Sites flanked by (AT)n appear to be bound better than those surrounded by An · Tn. Although no footprints are produced at T9GCA9 and T15CGA15, DNase I cleavage is enhanced with the GC sites suggesting that there is some interaction with the ligand. Mithramycin also alters the DNase I cleavage of (GA)n · (CT)n.</description><subject>Adenine - chemistry</subject><subject>Base Sequence</subject><subject>Binding Sites</subject><subject>Carbohydrate Sequence</subject><subject>Cytosine - chemistry</subject><subject>Deoxyribonuclease I</subject><subject>DNA - chemistry</subject><subject>DNase I footprinting</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Guanine - chemistry</subject><subject>Hydroxyl Radical</subject><subject>Minor groove binding</subject><subject>Mithramycin</subject><subject>Molecular Sequence Data</subject><subject>Molecular Structure</subject><subject>Plicamycin - chemistry</subject><subject>Sequence recognition</subject><subject>Thymine - chemistry</subject><issn>0952-3499</issn><issn>1099-1352</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kM1LAzEQxYMotVaPHoU9eds6SXY3m6MUra1VoVTqLWSTLKbuhyZbav97Iy3Fk3OZgfebx-MhdIlhiAHIzap2QwoADChkR6iPgfMY05Qcoz7wlMQ04fwUnXm_ChTnKfRQj-U5pAnto3zSdMZJ1dm2idoyqm337mS9VbaJNuGOrG8r2RkdjUeRbHQ0Gkfedsafo5NSVt5c7PcAvd7fLUYP8exlPBndzmJFcp7FmmkmU8406NIoggtTgNIhUsIKTTEGlVNCSZHkVGU44wnRNMNFGp7LlGZAB-h65_vp2q-18Z2orVemqmRj2rUXLAxNEhLAeAcq13rvTCk-na2l2woM4rcpEZoSh6YCf7U3Xhe10Qd6X03Q2U7f2Mps_zcT06f5X-d9Eus78334lO5DZIyyVCyfx-JtunhcLhkTc_oDGyuBhg</recordid><startdate>199409</startdate><enddate>199409</enddate><creator>Carpenter, Mark L.</creator><creator>Cassidy, Sarah A.</creator><creator>Fox, Keith R.</creator><general>John Wiley & Sons, Ltd</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>7X8</scope></search><sort><creationdate>199409</creationdate><title>Interaction of mithramycin with isolated GC and CG sites</title><author>Carpenter, Mark L. ; Cassidy, Sarah A. ; Fox, Keith R.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c2896-d7d7a597d0dfec21beb0cd34947bd3110c83232b483c616942d361b5289f53603</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Adenine - chemistry</topic><topic>Base Sequence</topic><topic>Binding Sites</topic><topic>Carbohydrate Sequence</topic><topic>Cytosine - chemistry</topic><topic>Deoxyribonuclease I</topic><topic>DNA - chemistry</topic><topic>DNase I footprinting</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Guanine - chemistry</topic><topic>Hydroxyl Radical</topic><topic>Minor groove binding</topic><topic>Mithramycin</topic><topic>Molecular Sequence Data</topic><topic>Molecular Structure</topic><topic>Plicamycin - chemistry</topic><topic>Sequence recognition</topic><topic>Thymine - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Carpenter, Mark L.</creatorcontrib><creatorcontrib>Cassidy, Sarah A.</creatorcontrib><creatorcontrib>Fox, Keith R.</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>MEDLINE - Academic</collection><jtitle>Journal of molecular recognition</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Carpenter, Mark L.</au><au>Cassidy, Sarah A.</au><au>Fox, Keith R.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Interaction of mithramycin with isolated GC and CG sites</atitle><jtitle>Journal of molecular recognition</jtitle><addtitle>J. Mol. Recognit</addtitle><date>1994-09</date><risdate>1994</risdate><volume>7</volume><issue>3</issue><spage>189</spage><epage>197</epage><pages>189-197</pages><issn>0952-3499</issn><eissn>1099-1352</eissn><abstract>We have studied the interaction of the GC‐specific, minor groove‐binding ligand, mithramycin, with cloned DNA inserts containing isolated GC and CG sites flanked by regions of (AT)n and An · Tn using DNase I and hydroxyl radical footprinting. We find that mithramycin binds to GC better than CG and that AGCT is a better site than TGCA. Sites flanked by (AT)n appear to be bound better than those surrounded by An · Tn. Although no footprints are produced at T9GCA9 and T15CGA15, DNase I cleavage is enhanced with the GC sites suggesting that there is some interaction with the ligand. Mithramycin also alters the DNase I cleavage of (GA)n · (CT)n.</abstract><cop>Chichester, UK</cop><pub>John Wiley & Sons, Ltd</pub><pmid>7880543</pmid><doi>10.1002/jmr.300070306</doi><tpages>9</tpages></addata></record> |
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| identifier | ISSN: 0952-3499 |
| ispartof | Journal of molecular recognition, 1994-09, Vol.7 (3), p.189-197 |
| issn | 0952-3499 1099-1352 |
| language | eng |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete |
| subjects | Adenine - chemistry Base Sequence Binding Sites Carbohydrate Sequence Cytosine - chemistry Deoxyribonuclease I DNA - chemistry DNase I footprinting Electrophoresis, Polyacrylamide Gel Guanine - chemistry Hydroxyl Radical Minor groove binding Mithramycin Molecular Sequence Data Molecular Structure Plicamycin - chemistry Sequence recognition Thymine - chemistry |
| title | Interaction of mithramycin with isolated GC and CG sites |
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