Interaction of Escherichia coli RNA polymerase holoenzyme containing σ32 with heat shock promoters: DNase I footprinting and methylation protection
The DNase I protection pattern of Eσ32 was assayed on three heat shock promoters, the Eσ32 promoter for the groESL operon, P2 of the dnaKJ operon, and rpoD PHS, the Eσ32 promoter upstream from rpoD. Eσ32 protected each of these promoters from DNase I digestion from around −60 to around +20. Protecti...
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| Veröffentlicht in: | Journal of molecular biology 1989-12, Vol.210 (3), p.513-520 |
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| creator | Cowing, Deborah W. Gross, Carol A. |
| description | The DNase I protection pattern of Eσ32 was assayed on three heat shock promoters, the Eσ32 promoter for the groESL operon, P2 of the dnaKJ operon, and rpoD PHS, the Eσ32 promoter upstream from rpoD. Eσ32 protected each of these promoters from DNase I digestion from around −60 to around +20. Protection from dimethyl sulfate methylation was assayed at the groE promoter. Eσ32 binding altered the sensitivity to methylation of bases in the vicinity of both the −10 and −35 regions.
The DNase I footprints for the Eσ32 promoters were very similar to the DNase I footprint of Eσ70 on the lacUV5 promoter. After analyzing the DNase I footprints by taking into account the contacts predicted to be made by DNase I, it appeared that Eσ32, like Eσ70, contacts the DNA primarily on one face of the helix in the −35 region and on both faces in the −10 region. |
| doi_str_mv | 10.1016/0022-2836(89)90127-7 |
| format | Article |
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The DNase I footprints for the Eσ32 promoters were very similar to the DNase I footprint of Eσ70 on the lacUV5 promoter. After analyzing the DNase I footprints by taking into account the contacts predicted to be made by DNase I, it appeared that Eσ32, like Eσ70, contacts the DNA primarily on one face of the helix in the −35 region and on both faces in the −10 region.</description><identifier>ISSN: 0022-2836</identifier><identifier>EISSN: 1089-8638</identifier><identifier>DOI: 10.1016/0022-2836(89)90127-7</identifier><identifier>CODEN: JMOBAK</identifier><language>eng</language><publisher>Oxford: Elsevier Ltd</publisher><subject>Biological and medical sciences ; Fundamental and applied biological sciences. Psychology ; Molecular and cellular biology ; Molecular genetics ; Transcription. Transcription factor. Splicing. Rna processing</subject><ispartof>Journal of molecular biology, 1989-12, Vol.210 (3), p.513-520</ispartof><rights>1989</rights><rights>1990 INIST-CNRS</rights><lds50>peer_reviewed</lds50><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/0022283689901277$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=6727155$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>Cowing, Deborah W.</creatorcontrib><creatorcontrib>Gross, Carol A.</creatorcontrib><title>Interaction of Escherichia coli RNA polymerase holoenzyme containing σ32 with heat shock promoters: DNase I footprinting and methylation protection</title><title>Journal of molecular biology</title><description>The DNase I protection pattern of Eσ32 was assayed on three heat shock promoters, the Eσ32 promoter for the groESL operon, P2 of the dnaKJ operon, and rpoD PHS, the Eσ32 promoter upstream from rpoD. Eσ32 protected each of these promoters from DNase I digestion from around −60 to around +20. Protection from dimethyl sulfate methylation was assayed at the groE promoter. Eσ32 binding altered the sensitivity to methylation of bases in the vicinity of both the −10 and −35 regions.
The DNase I footprints for the Eσ32 promoters were very similar to the DNase I footprint of Eσ70 on the lacUV5 promoter. After analyzing the DNase I footprints by taking into account the contacts predicted to be made by DNase I, it appeared that Eσ32, like Eσ70, contacts the DNA primarily on one face of the helix in the −35 region and on both faces in the −10 region.</description><subject>Biological and medical sciences</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Molecular and cellular biology</subject><subject>Molecular genetics</subject><subject>Transcription. Transcription factor. Splicing. Rna processing</subject><issn>0022-2836</issn><issn>1089-8638</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1989</creationdate><recordtype>article</recordtype><recordid>eNo9kc9u2zAMxoWhBZZme4MddOihPXijJP-ReyhQZOkWIEiBIndBlularSMFltAiu-4V9l59pcnJsBNJ8Efyw0dCvjD4yoCV3wA4z7gU5ZWsr2tgvMqqD2TGQNaZLIU8I7P_yEdyEcIzABQilzPyZ-UijtpE6x31HV0G0-NoTW81NX6w9HFzR_d-OOwSFZD2fvDofqUytV3U1ln3RN9_C07fbOxpjzrS0HvzQvej3_m0PNzQ75tpdkU77-N-tC5OQ9q1dIexPwz6eD3xEY9CPpHzTg8BP_-Lc7K9X24XP7P1w4_V4m6docyLrGt4XjZc57wTsmmqssgbAS10FaS0Zdgw4LKQDEVeCc50iwUwA5pxqFFwMSeXp7V7HYweulE7Y4NKAnd6PKiy4hUrioTdnjBMUl4tjioYi85ga8ekV7XeKgZq-oSabFaTzUrW6vgJVYm_bKN_IQ</recordid><startdate>19891205</startdate><enddate>19891205</enddate><creator>Cowing, Deborah W.</creator><creator>Gross, Carol A.</creator><general>Elsevier Ltd</general><general>Elsevier</general><scope>IQODW</scope></search><sort><creationdate>19891205</creationdate><title>Interaction of Escherichia coli RNA polymerase holoenzyme containing σ32 with heat shock promoters: DNase I footprinting and methylation protection</title><author>Cowing, Deborah W. ; Gross, Carol A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-e845-fb246b2a42f38bb7654b30d0f70654d1eb1028581e347321ade501c0a1209e323</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>Biological and medical sciences</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Molecular and cellular biology</topic><topic>Molecular genetics</topic><topic>Transcription. Transcription factor. Splicing. Rna processing</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Cowing, Deborah W.</creatorcontrib><creatorcontrib>Gross, Carol A.</creatorcontrib><collection>Pascal-Francis</collection><jtitle>Journal of molecular biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Cowing, Deborah W.</au><au>Gross, Carol A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Interaction of Escherichia coli RNA polymerase holoenzyme containing σ32 with heat shock promoters: DNase I footprinting and methylation protection</atitle><jtitle>Journal of molecular biology</jtitle><date>1989-12-05</date><risdate>1989</risdate><volume>210</volume><issue>3</issue><spage>513</spage><epage>520</epage><pages>513-520</pages><issn>0022-2836</issn><eissn>1089-8638</eissn><coden>JMOBAK</coden><abstract>The DNase I protection pattern of Eσ32 was assayed on three heat shock promoters, the Eσ32 promoter for the groESL operon, P2 of the dnaKJ operon, and rpoD PHS, the Eσ32 promoter upstream from rpoD. Eσ32 protected each of these promoters from DNase I digestion from around −60 to around +20. Protection from dimethyl sulfate methylation was assayed at the groE promoter. Eσ32 binding altered the sensitivity to methylation of bases in the vicinity of both the −10 and −35 regions.
The DNase I footprints for the Eσ32 promoters were very similar to the DNase I footprint of Eσ70 on the lacUV5 promoter. After analyzing the DNase I footprints by taking into account the contacts predicted to be made by DNase I, it appeared that Eσ32, like Eσ70, contacts the DNA primarily on one face of the helix in the −35 region and on both faces in the −10 region.</abstract><cop>Oxford</cop><pub>Elsevier Ltd</pub><doi>10.1016/0022-2836(89)90127-7</doi><tpages>8</tpages></addata></record> |
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| source | Elsevier ScienceDirect Journals |
| subjects | Biological and medical sciences Fundamental and applied biological sciences. Psychology Molecular and cellular biology Molecular genetics Transcription. Transcription factor. Splicing. Rna processing |
| title | Interaction of Escherichia coli RNA polymerase holoenzyme containing σ32 with heat shock promoters: DNase I footprinting and methylation protection |
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