T4 RNA ligase catalyzes the synthesis of dinucleoside polyphosphates
10 pages, 7 figures.-- Journal now known as FEBS Journal.-- Open Access: Content older than 1 year.
| Autores: | , , , |
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| Tipo de recurso: | artículo |
| Fecha de publicación: | 1999 |
| País: | España |
| Institución: | Consejo Superior de Investigaciones Científicas (CSIC) |
| Repositorio: | DIGITAL.CSIC. Repositorio Institucional del CSIC |
| OAI Identifier: | oai:digital.csic.es:10261/24355 |
| Acceso en línea: | http://hdl.handle.net/10261/24355 |
| Access Level: | acceso abierto |
| Palabra clave: | RNA ligase Dinucleoside polyphosphates Ap3A RNA joining |
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T4 RNA ligase catalyzes the synthesis of dinucleoside polyphosphatesAtencia, Eva AnaMadrid, OlgaGünther Sillero, María A.Sillero, AntonioRNA ligaseDinucleoside polyphosphatesAp3ARNA joining10 pages, 7 figures.-- Journal now known as FEBS Journal.-- Open Access: Content older than 1 year.T4 RNA ligase has been shown to synthesize nucleoside and dinucleoside 5'-polyphosphates by displacement of the AMP from the E-AMP complex with polyphosphates and nucleoside diphosphates and triphosphates. Displacement of the AMP by tripolyphosphate (P3) was concentration dependent, as measured by SDS/PAGE. When the enzyme was incubated in the presence of 0.02 mm[α-32P] ATP, synthesis of labeled Ap4A was observed: ATP was acting as both donor (Km, µm) and acceptor (Km, mm) of AMP from the enzyme. Whereas, as previously known, ATP or dATP (but not other nucleotides) were able to form the E-AMP complex, the specificity of a compound to be acceptor of AMP from the E-AMP complex was very broad, and with Km values between 1 and 2 mm. In the presence of a low concentration (0.02 mm) of [α-32P] ATP (enough to form the E-AMP complex, but only marginally enough to form Ap4A) and 4 mm of the indicated nucleotides or P3, the relative rate of synthesis of the following radioactive (di)nucleotides was observed: Ap4X (from XTP, 100); Ap4dG (from dGTP, 74); Ap4G (from GTP, 49); Ap4dC (from dCTP, 23); Ap4C (from CTP, 9); Ap3A (from ADP, 5); Ap4ddA, (from ddATP, 1); p4A (from P3, 200). The enzyme also synthesized efficiently Ap3A in the presence of 1 mm ATP and 2 mm ADP. The following T4 RNA ligase donors were inhibitors of the synthesis of Ap4G: pCp > pAp > pA2'p.This investigation was supported by grants from the Dirección General de Investigación Científica y Técnica (PM95/13) and Comunidad de Madrid (08.9/0004/1998).Peer reviewedWiley-Blackwell201020101999info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_65011026951 bytesapplication/pdfhttp://hdl.handle.net/10261/24355reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Ingléshttp://dx.doi.org/10.1046/j.1432-1327.1999.00338.xinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/243552026-05-22T06:33:51Z |
| dc.title.none.fl_str_mv |
T4 RNA ligase catalyzes the synthesis of dinucleoside polyphosphates |
| title |
T4 RNA ligase catalyzes the synthesis of dinucleoside polyphosphates |
| spellingShingle |
T4 RNA ligase catalyzes the synthesis of dinucleoside polyphosphates Atencia, Eva Ana RNA ligase Dinucleoside polyphosphates Ap3A RNA joining |
| title_short |
T4 RNA ligase catalyzes the synthesis of dinucleoside polyphosphates |
| title_full |
T4 RNA ligase catalyzes the synthesis of dinucleoside polyphosphates |
| title_fullStr |
T4 RNA ligase catalyzes the synthesis of dinucleoside polyphosphates |
| title_full_unstemmed |
T4 RNA ligase catalyzes the synthesis of dinucleoside polyphosphates |
| title_sort |
T4 RNA ligase catalyzes the synthesis of dinucleoside polyphosphates |
| dc.creator.none.fl_str_mv |
Atencia, Eva Ana Madrid, Olga Günther Sillero, María A. Sillero, Antonio |
| author |
Atencia, Eva Ana |
| author_facet |
Atencia, Eva Ana Madrid, Olga Günther Sillero, María A. Sillero, Antonio |
| author_role |
author |
| author2 |
Madrid, Olga Günther Sillero, María A. Sillero, Antonio |
| author2_role |
author author author |
| dc.subject.none.fl_str_mv |
RNA ligase Dinucleoside polyphosphates Ap3A RNA joining |
| topic |
RNA ligase Dinucleoside polyphosphates Ap3A RNA joining |
| description |
10 pages, 7 figures.-- Journal now known as FEBS Journal.-- Open Access: Content older than 1 year. |
| publishDate |
1999 |
| dc.date.none.fl_str_mv |
1999 2010 2010 |
| dc.type.none.fl_str_mv |
info:eu-repo/semantics/article http://purl.org/coar/resource_type/c_6501 |
| format |
article |
| dc.identifier.none.fl_str_mv |
http://hdl.handle.net/10261/24355 |
| url |
http://hdl.handle.net/10261/24355 |
| dc.language.none.fl_str_mv |
Inglés |
| language_invalid_str_mv |
Inglés |
| dc.relation.none.fl_str_mv |
http://dx.doi.org/10.1046/j.1432-1327.1999.00338.x |
| dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess |
| eu_rights_str_mv |
openAccess |
| dc.format.none.fl_str_mv |
1026951 bytes application/pdf |
| dc.publisher.none.fl_str_mv |
Wiley-Blackwell |
| publisher.none.fl_str_mv |
Wiley-Blackwell |
| dc.source.none.fl_str_mv |
reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC instname:Consejo Superior de Investigaciones Científicas (CSIC) |
| instname_str |
Consejo Superior de Investigaciones Científicas (CSIC) |
| reponame_str |
DIGITAL.CSIC. Repositorio Institucional del CSIC |
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DIGITAL.CSIC. Repositorio Institucional del CSIC |
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1869404344192860160 |
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15,811543 |