Effects of molecular crowding on the interaction between DNA and the Escherichia coli regulatory protein TyrR
Fluorescence quenching has been used to measure quantitatively the effects of sucrose and triethylene glycol on the interaction between the Escherichia coli regulatory protein TyrR and a 30-basepair oligonucleotide containing the strong TyrR box of the TyrR operon. It was observed that the apparent...
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| Veröffentlicht in: | Biophysical journal 1997-12, Vol.73 (6), p.3257-3264 |
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| container_end_page | 3264 |
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| container_issue | 6 |
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| container_title | Biophysical journal |
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| creator | Poon, J. Bailey, M. Winzor, D.J. Davidson, B.E. Sawyer, W.H. |
| description | Fluorescence quenching has been used to measure quantitatively the effects of sucrose and triethylene glycol on the interaction between the Escherichia coli regulatory protein TyrR and a 30-basepair oligonucleotide containing the strong TyrR box of the TyrR operon. It was observed that the apparent binding constant increased in the presence of co-solutes, the dependence of the logarithm of the apparent binding constant on molar concentration being indistinguishable and essentially linear for both co-solutes. This activation of the TyrR-oligonucleotide interaction is attributed to thermodynamic nonideality arising from molecular crowding, an interpretation which is supported by the reasonable agreement observed between the experimental extent of reaction enhancement and that predicted on the statistical-mechanical basis of excluded volume. |
| doi_str_mv | 10.1016/S0006-3495(97)78350-4 |
| format | Article |
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It was observed that the apparent binding constant increased in the presence of co-solutes, the dependence of the logarithm of the apparent binding constant on molar concentration being indistinguishable and essentially linear for both co-solutes. This activation of the TyrR-oligonucleotide interaction is attributed to thermodynamic nonideality arising from molecular crowding, an interpretation which is supported by the reasonable agreement observed between the experimental extent of reaction enhancement and that predicted on the statistical-mechanical basis of excluded volume.</description><identifier>ISSN: 0006-3495</identifier><identifier>EISSN: 1542-0086</identifier><identifier>DOI: 10.1016/S0006-3495(97)78350-4</identifier><identifier>PMID: 9414236</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Base Sequence ; Biophysical Phenomena ; Biophysics ; DNA, Bacterial - chemistry ; DNA, Bacterial - genetics ; DNA, Bacterial - metabolism ; Escherichia coli - genetics ; Escherichia coli - metabolism ; Escherichia coli Proteins ; Kinetics ; Macromolecular Substances ; Operon ; Osmotic Pressure ; Protein Binding ; Repressor Proteins - chemistry ; Repressor Proteins - genetics ; Repressor Proteins - metabolism ; Spectrometry, Fluorescence ; Thermodynamics</subject><ispartof>Biophysical journal, 1997-12, Vol.73 (6), p.3257-3264</ispartof><rights>1997 The Biophysical Society</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c528t-42b04da31c051a28ad176c962ad063ddabde30d1f50132a00c7ec2789ad25db23</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1181227/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0006-3495(97)78350-4$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,3550,27924,27925,45995,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9414236$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Poon, J.</creatorcontrib><creatorcontrib>Bailey, M.</creatorcontrib><creatorcontrib>Winzor, D.J.</creatorcontrib><creatorcontrib>Davidson, B.E.</creatorcontrib><creatorcontrib>Sawyer, W.H.</creatorcontrib><title>Effects of molecular crowding on the interaction between DNA and the Escherichia coli regulatory protein TyrR</title><title>Biophysical journal</title><addtitle>Biophys J</addtitle><description>Fluorescence quenching has been used to measure quantitatively the effects of sucrose and triethylene glycol on the interaction between the Escherichia coli regulatory protein TyrR and a 30-basepair oligonucleotide containing the strong TyrR box of the TyrR operon. It was observed that the apparent binding constant increased in the presence of co-solutes, the dependence of the logarithm of the apparent binding constant on molar concentration being indistinguishable and essentially linear for both co-solutes. This activation of the TyrR-oligonucleotide interaction is attributed to thermodynamic nonideality arising from molecular crowding, an interpretation which is supported by the reasonable agreement observed between the experimental extent of reaction enhancement and that predicted on the statistical-mechanical basis of excluded volume.</description><subject>Base Sequence</subject><subject>Biophysical Phenomena</subject><subject>Biophysics</subject><subject>DNA, Bacterial - chemistry</subject><subject>DNA, Bacterial - genetics</subject><subject>DNA, Bacterial - metabolism</subject><subject>Escherichia coli - genetics</subject><subject>Escherichia coli - metabolism</subject><subject>Escherichia coli Proteins</subject><subject>Kinetics</subject><subject>Macromolecular Substances</subject><subject>Operon</subject><subject>Osmotic Pressure</subject><subject>Protein Binding</subject><subject>Repressor Proteins - chemistry</subject><subject>Repressor Proteins - genetics</subject><subject>Repressor Proteins - metabolism</subject><subject>Spectrometry, Fluorescence</subject><subject>Thermodynamics</subject><issn>0006-3495</issn><issn>1542-0086</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU1vEzEQhi0EKqHwEyr5hOCwMP7YrwuoKmlBqkCCcra89mxitGsH22mVf4-bRBGcOI1G7zvv2PMQcsHgHQPWvP8BAE0lZF-_6du3bSdqqOQTsmC15BVA1zwli5PlOXmR0i8AxmtgZ-Ssl0xy0SzIvBxHNDnRMNI5TGi2k47UxPBgnV_R4GleI3U-Y9Qmu9IPmB8QPf309ZJqb_f6Mpk1RmfWTlMTJkcjrkpQDnFHNzFkdJ7e7eL3l-TZqKeEr471nPy8Xt5dfa5uv918ubq8rUzNu1xJPoC0WjADNdO805a1jekbri00wlo9WBRg2Vg-I7gGMC0a3na9try2Axfn5MMhd7MdZrQGfY56UpvoZh13Kmin_lW8W6tVuFeMdYzztgS8PgbE8HuLKavZJYPTpD2GbVJtLzvBWijG-mAsJ0sp4nhawkA9clJ7TuoRgupbteekZJm7-PuFp6kjmKJ_POhYznTvMKpkHHqD1sXCS9ng_rPhD1jwpQE</recordid><startdate>19971201</startdate><enddate>19971201</enddate><creator>Poon, J.</creator><creator>Bailey, M.</creator><creator>Winzor, D.J.</creator><creator>Davidson, B.E.</creator><creator>Sawyer, W.H.</creator><general>Elsevier Inc</general><scope>6I.</scope><scope>AAFTH</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><scope>5PM</scope></search><sort><creationdate>19971201</creationdate><title>Effects of molecular crowding on the interaction between DNA and the Escherichia coli regulatory protein TyrR</title><author>Poon, J. ; Bailey, M. ; Winzor, D.J. ; Davidson, B.E. ; Sawyer, W.H.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c528t-42b04da31c051a28ad176c962ad063ddabde30d1f50132a00c7ec2789ad25db23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>Base Sequence</topic><topic>Biophysical Phenomena</topic><topic>Biophysics</topic><topic>DNA, Bacterial - chemistry</topic><topic>DNA, Bacterial - genetics</topic><topic>DNA, Bacterial - metabolism</topic><topic>Escherichia coli - genetics</topic><topic>Escherichia coli - metabolism</topic><topic>Escherichia coli Proteins</topic><topic>Kinetics</topic><topic>Macromolecular Substances</topic><topic>Operon</topic><topic>Osmotic Pressure</topic><topic>Protein Binding</topic><topic>Repressor Proteins - chemistry</topic><topic>Repressor Proteins - genetics</topic><topic>Repressor Proteins - metabolism</topic><topic>Spectrometry, Fluorescence</topic><topic>Thermodynamics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Poon, J.</creatorcontrib><creatorcontrib>Bailey, M.</creatorcontrib><creatorcontrib>Winzor, D.J.</creatorcontrib><creatorcontrib>Davidson, B.E.</creatorcontrib><creatorcontrib>Sawyer, W.H.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</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><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biophysical journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Poon, J.</au><au>Bailey, M.</au><au>Winzor, D.J.</au><au>Davidson, B.E.</au><au>Sawyer, W.H.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Effects of molecular crowding on the interaction between DNA and the Escherichia coli regulatory protein TyrR</atitle><jtitle>Biophysical journal</jtitle><addtitle>Biophys J</addtitle><date>1997-12-01</date><risdate>1997</risdate><volume>73</volume><issue>6</issue><spage>3257</spage><epage>3264</epage><pages>3257-3264</pages><issn>0006-3495</issn><eissn>1542-0086</eissn><abstract>Fluorescence quenching has been used to measure quantitatively the effects of sucrose and triethylene glycol on the interaction between the Escherichia coli regulatory protein TyrR and a 30-basepair oligonucleotide containing the strong TyrR box of the TyrR operon. It was observed that the apparent binding constant increased in the presence of co-solutes, the dependence of the logarithm of the apparent binding constant on molar concentration being indistinguishable and essentially linear for both co-solutes. This activation of the TyrR-oligonucleotide interaction is attributed to thermodynamic nonideality arising from molecular crowding, an interpretation which is supported by the reasonable agreement observed between the experimental extent of reaction enhancement and that predicted on the statistical-mechanical basis of excluded volume.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>9414236</pmid><doi>10.1016/S0006-3495(97)78350-4</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Cell Press Free Archives; Access via ScienceDirect (Elsevier); EZB-FREE-00999 freely available EZB journals; PubMed Central |
| subjects | Base Sequence Biophysical Phenomena Biophysics DNA, Bacterial - chemistry DNA, Bacterial - genetics DNA, Bacterial - metabolism Escherichia coli - genetics Escherichia coli - metabolism Escherichia coli Proteins Kinetics Macromolecular Substances Operon Osmotic Pressure Protein Binding Repressor Proteins - chemistry Repressor Proteins - genetics Repressor Proteins - metabolism Spectrometry, Fluorescence Thermodynamics |
| title | Effects of molecular crowding on the interaction between DNA and the Escherichia coli regulatory protein TyrR |
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