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Authordc.contributor.authorAcevedo Acevedo, Mónica 
Authordc.contributor.authorArbildua, José J. es_CL
Authordc.contributor.authorMonasterio Opazo, Octavio es_CL
Authordc.contributor.authorToledo Araya, Héctor es_CL
Authordc.contributor.authorLeón Decap, Oscar es_CL
Admission datedc.date.accessioned2010-06-14T18:58:03Z
Available datedc.date.available2010-06-14T18:58:03Z
Publication datedc.date.issued2010
Cita de ítemdc.identifier.citationArchives of Biochemistry and Biophysics 495 (2010) 28–34en_US
Identifierdc.identifier.otherdoi:10.1016/j.abb.2009.12.018
Identifierdc.identifier.urihttps://repositorio.uchile.cl/handle/2250/128544
Abstractdc.description.abstractX-ray diffraction data on a few retroviral integrases show a flexible loop near the active site. By sequence alignment, the peptide region 207–218 of Mo-MLV IN appears to correspond to this flexible loop. In this study, residues H208, Y211, R212, Q214, S215 and S216 of Mo-MLV IN were mutated to determine their role on enzyme activity. We found that Y211A, R212A, R212K and Q214A decreased integration activity, while disintegration and 30-processing were not significantly affected. By contrast H208A was completely inactive in all the assays. The core domain of Mo-MLV integrase was modeled and the flexibility of the region 207–216 was analyzed. Substitutions with low integration activity showed a lower flexibility than wild type integrase. We propose that the peptide region 207–216 is a flexible loop and that H208, Y211, R212 and Q214 of this loop are involved in the correct assembly of the DNA-integrase complex during integration.en_US
Patrocinadordc.description.sponsorshipThis work was funded by grant Fondecyt 1040409.en_US
Lenguagedc.language.isoenen_US
Publisherdc.publisherELSEVIERen_US
Keywordsdc.subjectIntegraseen_US
Títulodc.titleRole of the 207–218 peptide region of Moloney murine leukemia virus integrase in enzyme catalysisen_US
Document typedc.typeArtículo de revista


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