Nuclease footprinting of human immunodeficiency virus reverse transcriptase/tRNA(Lys-3) complexes
Nuclease footprinting has been used to probe features of binary complexes of type 1 human immunodeficiency virus reverse transcriptase (HIV-1 RT) with both natural and synthetic preparations of its cognate replication primer, tRNA(Lys-3). In addition to heterodimeric RT (p66/p51), ribonucleoprotein...
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| Veröffentlicht in: | The Journal of biological chemistry 1993-06, Vol.268 (18), p.13617-13624 |
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| container_issue | 18 |
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| container_title | The Journal of biological chemistry |
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| creator | Wöhrl, B M Ehresmann, B Keith, G Le Grice, S F |
| description | Nuclease footprinting has been used to probe features of binary complexes of type 1 human immunodeficiency virus reverse transcriptase
(HIV-1 RT) with both natural and synthetic preparations of its cognate replication primer, tRNA(Lys-3). In addition to heterodimeric
RT (p66/p51), ribonucleoprotein complexes containing either the p66 or p51 subunit were analyzed. Footprinting experiments
employed both structure- and sequence-specific nucleases. Our results indicate a similar mode of interaction for the three
RT preparations tested, suggesting contact with each loop of the tRNA primer (D, anticodon, and T psi C), as well as minor
perturbation of the anticodon stem. Although there is little evidence for extensive disruption of the 3'-acceptor stem. RNase
A footprinting data with natural and synthetic tRNA suggests that potential base pairing between the T psi C and D loops is
disrupted in the presence of RT. |
| doi_str_mv | 10.1016/S0021-9258(19)38693-4 |
| format | Article |
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(HIV-1 RT) with both natural and synthetic preparations of its cognate replication primer, tRNA(Lys-3). In addition to heterodimeric
RT (p66/p51), ribonucleoprotein complexes containing either the p66 or p51 subunit were analyzed. Footprinting experiments
employed both structure- and sequence-specific nucleases. Our results indicate a similar mode of interaction for the three
RT preparations tested, suggesting contact with each loop of the tRNA primer (D, anticodon, and T psi C), as well as minor
perturbation of the anticodon stem. Although there is little evidence for extensive disruption of the 3'-acceptor stem. RNase
A footprinting data with natural and synthetic tRNA suggests that potential base pairing between the T psi C and D loops is
disrupted in the presence of RT.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(19)38693-4</identifier><identifier>PMID: 7685766</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>AIDS/HIV ; Anticodon ; Base Sequence ; HIV Reverse Transcriptase ; HIV-1 - enzymology ; Hydrolysis ; Molecular Sequence Data ; Nucleic Acid Conformation ; Recombinant Proteins - metabolism ; Ribonuclease, Pancreatic - metabolism ; RNA, Double-Stranded - metabolism ; RNA, Transfer, Lys - chemistry ; RNA, Transfer, Lys - metabolism ; RNA-Directed DNA Polymerase - metabolism</subject><ispartof>The Journal of biological chemistry, 1993-06, Vol.268 (18), p.13617-13624</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c2954-adbf4cb72a61ce2525e841f4588f18dd576053b22f4f403e9b92129851040cfa3</citedby><cites>FETCH-LOGICAL-c2954-adbf4cb72a61ce2525e841f4588f18dd576053b22f4f403e9b92129851040cfa3</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/7685766$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wöhrl, B M</creatorcontrib><creatorcontrib>Ehresmann, B</creatorcontrib><creatorcontrib>Keith, G</creatorcontrib><creatorcontrib>Le Grice, S F</creatorcontrib><title>Nuclease footprinting of human immunodeficiency virus reverse transcriptase/tRNA(Lys-3) complexes</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Nuclease footprinting has been used to probe features of binary complexes of type 1 human immunodeficiency virus reverse transcriptase
(HIV-1 RT) with both natural and synthetic preparations of its cognate replication primer, tRNA(Lys-3). In addition to heterodimeric
RT (p66/p51), ribonucleoprotein complexes containing either the p66 or p51 subunit were analyzed. Footprinting experiments
employed both structure- and sequence-specific nucleases. Our results indicate a similar mode of interaction for the three
RT preparations tested, suggesting contact with each loop of the tRNA primer (D, anticodon, and T psi C), as well as minor
perturbation of the anticodon stem. Although there is little evidence for extensive disruption of the 3'-acceptor stem. RNase
A footprinting data with natural and synthetic tRNA suggests that potential base pairing between the T psi C and D loops is
disrupted in the presence of RT.</description><subject>AIDS/HIV</subject><subject>Anticodon</subject><subject>Base Sequence</subject><subject>HIV Reverse Transcriptase</subject><subject>HIV-1 - enzymology</subject><subject>Hydrolysis</subject><subject>Molecular Sequence Data</subject><subject>Nucleic Acid Conformation</subject><subject>Recombinant Proteins - metabolism</subject><subject>Ribonuclease, Pancreatic - metabolism</subject><subject>RNA, Double-Stranded - metabolism</subject><subject>RNA, Transfer, Lys - chemistry</subject><subject>RNA, Transfer, Lys - metabolism</subject><subject>RNA-Directed DNA Polymerase - metabolism</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kFtr2zAUx0VZ6dLLRwj4YYzmwauutvRYytYOQgu9QN-ELB81GraVSXa2fPuqSagQ6OF_OUc_hOYE_yCYVFdPGFNSKirkJVELJivFSn6EZgRLVjJBXr-g2aflKzpN6Q_Ohytygk7qSoq6qmbI3E-2A5OgcCGM6-iH0Q9vRXDFaurNUPi-n4bQgvPWw2C3xcbHKRURNhBzaIxmSDb69ZgrrsbH--vL5TaVbFHY0K87-A_pHB070yW4OLxn6OXXz-ebu3L5cPv75npZWqoEL03bOG6bmpqKWKCCCpCcOC6kdES2bV4XC9ZQ6rjjmIFqFCVUSUEwx9YZdoa-73vXMfydII2698lC15kBwpR0LWrFuKyzUeyNNoaUIjidv92buNUE6w-0eodWf3DTROkdWs1zbn4YMDU9tJ-pA8usf9vrK_-2-ucj6MYHu4Je0yoX5csqUrN310OBQA</recordid><startdate>19930625</startdate><enddate>19930625</enddate><creator>Wöhrl, B M</creator><creator>Ehresmann, B</creator><creator>Keith, G</creator><creator>Le Grice, S F</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>7X8</scope></search><sort><creationdate>19930625</creationdate><title>Nuclease footprinting of human immunodeficiency virus reverse transcriptase/tRNA(Lys-3) complexes</title><author>Wöhrl, B M ; Ehresmann, B ; Keith, G ; Le Grice, S F</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c2954-adbf4cb72a61ce2525e841f4588f18dd576053b22f4f403e9b92129851040cfa3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>AIDS/HIV</topic><topic>Anticodon</topic><topic>Base Sequence</topic><topic>HIV Reverse Transcriptase</topic><topic>HIV-1 - enzymology</topic><topic>Hydrolysis</topic><topic>Molecular Sequence Data</topic><topic>Nucleic Acid Conformation</topic><topic>Recombinant Proteins - metabolism</topic><topic>Ribonuclease, Pancreatic - metabolism</topic><topic>RNA, Double-Stranded - metabolism</topic><topic>RNA, Transfer, Lys - chemistry</topic><topic>RNA, Transfer, Lys - metabolism</topic><topic>RNA-Directed DNA Polymerase - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wöhrl, B M</creatorcontrib><creatorcontrib>Ehresmann, B</creatorcontrib><creatorcontrib>Keith, G</creatorcontrib><creatorcontrib>Le Grice, S F</creatorcontrib><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>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wöhrl, B M</au><au>Ehresmann, B</au><au>Keith, G</au><au>Le Grice, S F</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Nuclease footprinting of human immunodeficiency virus reverse transcriptase/tRNA(Lys-3) complexes</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1993-06-25</date><risdate>1993</risdate><volume>268</volume><issue>18</issue><spage>13617</spage><epage>13624</epage><pages>13617-13624</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Nuclease footprinting has been used to probe features of binary complexes of type 1 human immunodeficiency virus reverse transcriptase
(HIV-1 RT) with both natural and synthetic preparations of its cognate replication primer, tRNA(Lys-3). In addition to heterodimeric
RT (p66/p51), ribonucleoprotein complexes containing either the p66 or p51 subunit were analyzed. Footprinting experiments
employed both structure- and sequence-specific nucleases. Our results indicate a similar mode of interaction for the three
RT preparations tested, suggesting contact with each loop of the tRNA primer (D, anticodon, and T psi C), as well as minor
perturbation of the anticodon stem. Although there is little evidence for extensive disruption of the 3'-acceptor stem. RNase
A footprinting data with natural and synthetic tRNA suggests that potential base pairing between the T psi C and D loops is
disrupted in the presence of RT.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>7685766</pmid><doi>10.1016/S0021-9258(19)38693-4</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 1993-06, Vol.268 (18), p.13617-13624 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_75793487 |
| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | AIDS/HIV Anticodon Base Sequence HIV Reverse Transcriptase HIV-1 - enzymology Hydrolysis Molecular Sequence Data Nucleic Acid Conformation Recombinant Proteins - metabolism Ribonuclease, Pancreatic - metabolism RNA, Double-Stranded - metabolism RNA, Transfer, Lys - chemistry RNA, Transfer, Lys - metabolism RNA-Directed DNA Polymerase - metabolism |
| title | Nuclease footprinting of human immunodeficiency virus reverse transcriptase/tRNA(Lys-3) complexes |
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