In Vitro Analysis of the Interaction between the FinO Protein and FinP Antisense RNA of F-like Conjugative Plasmids
The FinO protein regulates the transfer potential of F-like conjugative plasmids through its interaction with FinP antisense RNA and its target, traJ mRNA. FinO binds to and protects FinP from degradation and promotes duplex formation between FinP and traJ mRNA in vitro . The FinP secondary structur...
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| Veröffentlicht in: | The Journal of biological chemistry 1999-04, Vol.274 (15), p.10356-10362 |
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| container_title | The Journal of biological chemistry |
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| creator | Jerome, L J Frost, L S |
| description | The FinO protein regulates the transfer potential of F-like conjugative plasmids through its interaction with FinP antisense
RNA and its target, traJ mRNA. FinO binds to and protects FinP from degradation and promotes duplex formation between FinP and traJ mRNA in vitro . The FinP secondary structure consists of two stem-loop domains separated by a 4-base spacer and terminated by a 6-base tail.
Previous studies suggested FinO bound to the smooth 14-base pair helix of stem-loop II. In this investigation, RNA mobility
shift analysis was used to study the interaction between a glutathione S -transferase (GST)-FinO fusion protein and a series of synthetic FinP and traJ mRNA variants. Mutations in 16 of the 28 bases in stem II of FinP that are predicted to disrupt base pairing did not significantly
alter the GST-FinO binding affinity. Removal of the single-stranded regions on either side of stem-loop II led to a dramatic
decrease in GST-FinO binding to FinP and to the complementary region of the traJ mRNA leader. While no evidence for sequence-specific contacts was found, the results suggest that FinO recognizes the overall
shape of the RNA and is influenced by the length of the single-stranded regions flanking the stem-loop. |
| doi_str_mv | 10.1074/jbc.274.15.10356 |
| format | Article |
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RNA and its target, traJ mRNA. FinO binds to and protects FinP from degradation and promotes duplex formation between FinP and traJ mRNA in vitro . The FinP secondary structure consists of two stem-loop domains separated by a 4-base spacer and terminated by a 6-base tail.
Previous studies suggested FinO bound to the smooth 14-base pair helix of stem-loop II. In this investigation, RNA mobility
shift analysis was used to study the interaction between a glutathione S -transferase (GST)-FinO fusion protein and a series of synthetic FinP and traJ mRNA variants. Mutations in 16 of the 28 bases in stem II of FinP that are predicted to disrupt base pairing did not significantly
alter the GST-FinO binding affinity. Removal of the single-stranded regions on either side of stem-loop II led to a dramatic
decrease in GST-FinO binding to FinP and to the complementary region of the traJ mRNA leader. While no evidence for sequence-specific contacts was found, the results suggest that FinO recognizes the overall
shape of the RNA and is influenced by the length of the single-stranded regions flanking the stem-loop.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.274.15.10356</identifier><identifier>PMID: 10187824</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Bacterial Outer Membrane Proteins - genetics ; Bacterial Outer Membrane Proteins - metabolism ; Bacterial Proteins - metabolism ; Base Sequence ; Escherichia coli Proteins ; Molecular Sequence Data ; Nucleic Acid Conformation ; Oligonucleotides, Antisense - metabolism ; Plasmids - metabolism ; Repressor Proteins ; RNA, Antisense - genetics ; RNA, Bacterial - metabolism ; RNA, Messenger - metabolism ; RNA-Binding Proteins - metabolism ; Structure-Activity Relationship</subject><ispartof>The Journal of biological chemistry, 1999-04, Vol.274 (15), p.10356-10362</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c397t-e572ce06ce0501b5c609c8d1d7410132d4ea1fcdaaad7d3ec2a8049030a23d433</citedby><cites>FETCH-LOGICAL-c397t-e572ce06ce0501b5c609c8d1d7410132d4ea1fcdaaad7d3ec2a8049030a23d433</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/10187824$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Jerome, L J</creatorcontrib><creatorcontrib>Frost, L S</creatorcontrib><title>In Vitro Analysis of the Interaction between the FinO Protein and FinP Antisense RNA of F-like Conjugative Plasmids</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>The FinO protein regulates the transfer potential of F-like conjugative plasmids through its interaction with FinP antisense
RNA and its target, traJ mRNA. FinO binds to and protects FinP from degradation and promotes duplex formation between FinP and traJ mRNA in vitro . The FinP secondary structure consists of two stem-loop domains separated by a 4-base spacer and terminated by a 6-base tail.
Previous studies suggested FinO bound to the smooth 14-base pair helix of stem-loop II. In this investigation, RNA mobility
shift analysis was used to study the interaction between a glutathione S -transferase (GST)-FinO fusion protein and a series of synthetic FinP and traJ mRNA variants. Mutations in 16 of the 28 bases in stem II of FinP that are predicted to disrupt base pairing did not significantly
alter the GST-FinO binding affinity. Removal of the single-stranded regions on either side of stem-loop II led to a dramatic
decrease in GST-FinO binding to FinP and to the complementary region of the traJ mRNA leader. While no evidence for sequence-specific contacts was found, the results suggest that FinO recognizes the overall
shape of the RNA and is influenced by the length of the single-stranded regions flanking the stem-loop.</description><subject>Bacterial Outer Membrane Proteins - genetics</subject><subject>Bacterial Outer Membrane Proteins - metabolism</subject><subject>Bacterial Proteins - metabolism</subject><subject>Base Sequence</subject><subject>Escherichia coli Proteins</subject><subject>Molecular Sequence Data</subject><subject>Nucleic Acid Conformation</subject><subject>Oligonucleotides, Antisense - metabolism</subject><subject>Plasmids - metabolism</subject><subject>Repressor Proteins</subject><subject>RNA, Antisense - genetics</subject><subject>RNA, Bacterial - metabolism</subject><subject>RNA, Messenger - metabolism</subject><subject>RNA-Binding Proteins - metabolism</subject><subject>Structure-Activity Relationship</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc9LHDEYhoO01K327klyKL3NNr9mMnNclq5dkLqIlt5CJvnWzTqTaJJV_O-bdT3YUwMh5ON5XxIehM4omVIixfdtb6ZMiimty53XzRGaUNLyitf0zwc0IYTRqmN1e4w-p7QlZYmOfkLHlNBWtkxMUFp6_NvlGPDM6-EluYTDGucN4KXPELXJLnjcQ34G8K_zhfNXeBVDBuex9nY_WJV0dgl8Anz9a7avWFSDuwc8D367u9PZPQFeDTqNzqZT9HGthwRf3s4TdLv4cTP_WV1eXSzns8vK8E7mCmrJDJCm7JrQvjYN6UxrqZWivJ8zK0DTtbFaaystB8N0W_5HONGMW8H5Cfp26H2I4XEHKavRJQPDoD2EXVJN17RM0va_IJWMSC5EAckBNDGkFGGtHqIbdXxRlKi9EVWMqGJE0Vq9GimR87fuXT-CfRc4KCjA1wOwcXebZxdB9S6YDYz_9vwFdiySkA</recordid><startdate>19990409</startdate><enddate>19990409</enddate><creator>Jerome, L J</creator><creator>Frost, L S</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>7TM</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>19990409</creationdate><title>In Vitro Analysis of the Interaction between the FinO Protein and FinP Antisense RNA of F-like Conjugative Plasmids</title><author>Jerome, L J ; Frost, L S</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c397t-e572ce06ce0501b5c609c8d1d7410132d4ea1fcdaaad7d3ec2a8049030a23d433</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Bacterial Outer Membrane Proteins - genetics</topic><topic>Bacterial Outer Membrane Proteins - metabolism</topic><topic>Bacterial Proteins - metabolism</topic><topic>Base Sequence</topic><topic>Escherichia coli Proteins</topic><topic>Molecular Sequence Data</topic><topic>Nucleic Acid Conformation</topic><topic>Oligonucleotides, Antisense - metabolism</topic><topic>Plasmids - metabolism</topic><topic>Repressor Proteins</topic><topic>RNA, Antisense - genetics</topic><topic>RNA, Bacterial - metabolism</topic><topic>RNA, Messenger - metabolism</topic><topic>RNA-Binding Proteins - metabolism</topic><topic>Structure-Activity Relationship</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Jerome, L J</creatorcontrib><creatorcontrib>Frost, L S</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>Nucleic Acids Abstracts</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>Jerome, L J</au><au>Frost, L S</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>In Vitro Analysis of the Interaction between the FinO Protein and FinP Antisense RNA of F-like Conjugative Plasmids</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1999-04-09</date><risdate>1999</risdate><volume>274</volume><issue>15</issue><spage>10356</spage><epage>10362</epage><pages>10356-10362</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>The FinO protein regulates the transfer potential of F-like conjugative plasmids through its interaction with FinP antisense
RNA and its target, traJ mRNA. FinO binds to and protects FinP from degradation and promotes duplex formation between FinP and traJ mRNA in vitro . The FinP secondary structure consists of two stem-loop domains separated by a 4-base spacer and terminated by a 6-base tail.
Previous studies suggested FinO bound to the smooth 14-base pair helix of stem-loop II. In this investigation, RNA mobility
shift analysis was used to study the interaction between a glutathione S -transferase (GST)-FinO fusion protein and a series of synthetic FinP and traJ mRNA variants. Mutations in 16 of the 28 bases in stem II of FinP that are predicted to disrupt base pairing did not significantly
alter the GST-FinO binding affinity. Removal of the single-stranded regions on either side of stem-loop II led to a dramatic
decrease in GST-FinO binding to FinP and to the complementary region of the traJ mRNA leader. While no evidence for sequence-specific contacts was found, the results suggest that FinO recognizes the overall
shape of the RNA and is influenced by the length of the single-stranded regions flanking the stem-loop.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>10187824</pmid><doi>10.1074/jbc.274.15.10356</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Bacterial Outer Membrane Proteins - genetics Bacterial Outer Membrane Proteins - metabolism Bacterial Proteins - metabolism Base Sequence Escherichia coli Proteins Molecular Sequence Data Nucleic Acid Conformation Oligonucleotides, Antisense - metabolism Plasmids - metabolism Repressor Proteins RNA, Antisense - genetics RNA, Bacterial - metabolism RNA, Messenger - metabolism RNA-Binding Proteins - metabolism Structure-Activity Relationship |
| title | In Vitro Analysis of the Interaction between the FinO Protein and FinP Antisense RNA of F-like Conjugative Plasmids |
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