A Natively Unfolded Toxin Domain Uses Its Receptor as a Folding Template
Natively unfolded proteins range from molten globules to disordered coils. They are abundant in eukaryotic genomes and commonly involved in molecular interactions. The essential N-terminal translocation domains of colicin toxins from Escherichia coli are disordered bacterial proteins that bind at le...
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| Veröffentlicht in: | The Journal of biological chemistry 2004-05, Vol.279 (21), p.22002-22009 |
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| container_end_page | 22009 |
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| container_issue | 21 |
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| container_title | The Journal of biological chemistry |
| container_volume | 279 |
| creator | Anderluh, Gregor Gökçe, Isa Lakey, Jeremy H |
| description | Natively unfolded proteins range from molten globules to disordered coils. They are abundant in eukaryotic genomes and commonly
involved in molecular interactions. The essential N-terminal translocation domains of colicin toxins from Escherichia coli are disordered bacterial proteins that bind at least one protein of the Tol or Ton family. The colicin N translocation domain
(ColN-(1â90)), which binds to the C-terminal domain of TolA (TolA-(296â421)), shows a disordered far-UV CD spectrum, no near-UV
CD signal, and non-cooperative thermal unfolding. As expected, TolA-(296â421) displays both secondary structure in far-UV
CD and tertiary structure in near-UV CD. Furthermore it shows a cooperative unfolding transition at 65 °C. CD spectra of the
1:1 complex show both increased secondary structure and colicin N-specific near-UV CD signals. A new cooperative thermal transition
at 35 °C is followed by the unchanged unfolding behavior of TolA-(296â421). Fluorescence and surface plasmon resonance confirm
that the new unfolding transition accompanies dissociation of ColN-(1â90). Hence upon binding the disordered structure of
ColN-(1â90) converts to a cooperatively folded domain without altering the TolA-(296â421) structure. |
| doi_str_mv | 10.1074/jbc.M313603200 |
| format | Article |
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involved in molecular interactions. The essential N-terminal translocation domains of colicin toxins from Escherichia coli are disordered bacterial proteins that bind at least one protein of the Tol or Ton family. The colicin N translocation domain
(ColN-(1â90)), which binds to the C-terminal domain of TolA (TolA-(296â421)), shows a disordered far-UV CD spectrum, no near-UV
CD signal, and non-cooperative thermal unfolding. As expected, TolA-(296â421) displays both secondary structure in far-UV
CD and tertiary structure in near-UV CD. Furthermore it shows a cooperative unfolding transition at 65 °C. CD spectra of the
1:1 complex show both increased secondary structure and colicin N-specific near-UV CD signals. A new cooperative thermal transition
at 35 °C is followed by the unchanged unfolding behavior of TolA-(296â421). Fluorescence and surface plasmon resonance confirm
that the new unfolding transition accompanies dissociation of ColN-(1â90). Hence upon binding the disordered structure of
ColN-(1â90) converts to a cooperatively folded domain without altering the TolA-(296â421) structure.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M313603200</identifier><identifier>PMID: 15004032</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Chromatography, Gel ; Circular Dichroism ; Colicins - chemistry ; Escherichia coli ; Escherichia coli - metabolism ; Kinetics ; Microscopy, Fluorescence ; Protein Binding ; Protein Denaturation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Surface Plasmon Resonance ; Temperature ; Ultraviolet Rays</subject><ispartof>The Journal of biological chemistry, 2004-05, Vol.279 (21), p.22002-22009</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c391t-25acd14a1592b26fc625ef13701db3778ee8dee820829cec597a658620a591d53</citedby><cites>FETCH-LOGICAL-c391t-25acd14a1592b26fc625ef13701db3778ee8dee820829cec597a658620a591d53</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15004032$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Anderluh, Gregor</creatorcontrib><creatorcontrib>Gökçe, Isa</creatorcontrib><creatorcontrib>Lakey, Jeremy H</creatorcontrib><title>A Natively Unfolded Toxin Domain Uses Its Receptor as a Folding Template</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Natively unfolded proteins range from molten globules to disordered coils. They are abundant in eukaryotic genomes and commonly
involved in molecular interactions. The essential N-terminal translocation domains of colicin toxins from Escherichia coli are disordered bacterial proteins that bind at least one protein of the Tol or Ton family. The colicin N translocation domain
(ColN-(1â90)), which binds to the C-terminal domain of TolA (TolA-(296â421)), shows a disordered far-UV CD spectrum, no near-UV
CD signal, and non-cooperative thermal unfolding. As expected, TolA-(296â421) displays both secondary structure in far-UV
CD and tertiary structure in near-UV CD. Furthermore it shows a cooperative unfolding transition at 65 °C. CD spectra of the
1:1 complex show both increased secondary structure and colicin N-specific near-UV CD signals. A new cooperative thermal transition
at 35 °C is followed by the unchanged unfolding behavior of TolA-(296â421). Fluorescence and surface plasmon resonance confirm
that the new unfolding transition accompanies dissociation of ColN-(1â90). Hence upon binding the disordered structure of
ColN-(1â90) converts to a cooperatively folded domain without altering the TolA-(296â421) structure.</description><subject>Chromatography, Gel</subject><subject>Circular Dichroism</subject><subject>Colicins - chemistry</subject><subject>Escherichia coli</subject><subject>Escherichia coli - metabolism</subject><subject>Kinetics</subject><subject>Microscopy, Fluorescence</subject><subject>Protein Binding</subject><subject>Protein Denaturation</subject><subject>Protein Folding</subject><subject>Protein Structure, Secondary</subject><subject>Protein Structure, Tertiary</subject><subject>Surface Plasmon Resonance</subject><subject>Temperature</subject><subject>Ultraviolet Rays</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkD1PwzAQhi0EglJYGZEHxJbiO9dxPCKggMSHhFqJzXKcCw1KmhKnQP89Rq3EyEmnu-F53-Fh7ATECIQeX7znfvQoQaZCohA7bAAik4lU8LrLBkIgJAZVdsAOQ3gXccYG9tkBqPjFxIDdXfIn11efVK_5bFG2dUEFn7bf1YJft42LZxYo8Ps-8BfytOzbjrvAHZ9EtFq88Sk1y9r1dMT2SlcHOt7eIZtNbqZXd8nD8-391eVD4qWBPkHlfAFjB8pgjmnpU1RUgtQCilxqnRFlRVwUGRpPXhntUpWlKJwyUCg5ZOeb3mXXfqwo9Lapgqe6dgtqV8FqMGikTv8FQWeIkGEERxvQd20IHZV22VWN69YWhP2VbKNk-yc5Bk63zau8oeIP31qNwNkGmFdv86-qI5tXrZ9TY1Ebi2Ax1qD8AZEIgW4</recordid><startdate>20040521</startdate><enddate>20040521</enddate><creator>Anderluh, Gregor</creator><creator>Gökçe, Isa</creator><creator>Lakey, Jeremy H</creator><general>American Society for Biochemistry and Molecular Biology</general><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>C1K</scope><scope>7X8</scope></search><sort><creationdate>20040521</creationdate><title>A Natively Unfolded Toxin Domain Uses Its Receptor as a Folding Template</title><author>Anderluh, Gregor ; Gökçe, Isa ; Lakey, Jeremy H</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c391t-25acd14a1592b26fc625ef13701db3778ee8dee820829cec597a658620a591d53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Chromatography, Gel</topic><topic>Circular Dichroism</topic><topic>Colicins - chemistry</topic><topic>Escherichia coli</topic><topic>Escherichia coli - metabolism</topic><topic>Kinetics</topic><topic>Microscopy, Fluorescence</topic><topic>Protein Binding</topic><topic>Protein Denaturation</topic><topic>Protein Folding</topic><topic>Protein Structure, Secondary</topic><topic>Protein Structure, Tertiary</topic><topic>Surface Plasmon Resonance</topic><topic>Temperature</topic><topic>Ultraviolet Rays</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Anderluh, Gregor</creatorcontrib><creatorcontrib>Gökçe, Isa</creatorcontrib><creatorcontrib>Lakey, Jeremy H</creatorcontrib><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>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Anderluh, Gregor</au><au>Gökçe, Isa</au><au>Lakey, Jeremy H</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A Natively Unfolded Toxin Domain Uses Its Receptor as a Folding Template</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2004-05-21</date><risdate>2004</risdate><volume>279</volume><issue>21</issue><spage>22002</spage><epage>22009</epage><pages>22002-22009</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Natively unfolded proteins range from molten globules to disordered coils. They are abundant in eukaryotic genomes and commonly
involved in molecular interactions. The essential N-terminal translocation domains of colicin toxins from Escherichia coli are disordered bacterial proteins that bind at least one protein of the Tol or Ton family. The colicin N translocation domain
(ColN-(1â90)), which binds to the C-terminal domain of TolA (TolA-(296â421)), shows a disordered far-UV CD spectrum, no near-UV
CD signal, and non-cooperative thermal unfolding. As expected, TolA-(296â421) displays both secondary structure in far-UV
CD and tertiary structure in near-UV CD. Furthermore it shows a cooperative unfolding transition at 65 °C. CD spectra of the
1:1 complex show both increased secondary structure and colicin N-specific near-UV CD signals. A new cooperative thermal transition
at 35 °C is followed by the unchanged unfolding behavior of TolA-(296â421). Fluorescence and surface plasmon resonance confirm
that the new unfolding transition accompanies dissociation of ColN-(1â90). Hence upon binding the disordered structure of
ColN-(1â90) converts to a cooperatively folded domain without altering the TolA-(296â421) structure.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>15004032</pmid><doi>10.1074/jbc.M313603200</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 2004-05, Vol.279 (21), p.22002-22009 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_71929376 |
| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Chromatography, Gel Circular Dichroism Colicins - chemistry Escherichia coli Escherichia coli - metabolism Kinetics Microscopy, Fluorescence Protein Binding Protein Denaturation Protein Folding Protein Structure, Secondary Protein Structure, Tertiary Surface Plasmon Resonance Temperature Ultraviolet Rays |
| title | A Natively Unfolded Toxin Domain Uses Its Receptor as a Folding Template |
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