Expression, purification and structural analysis of the Pyrococcus abyssi RNA binding protein PAB1135

dc.creatorLuz, Juliana S
dc.creatorBarbosa, João ARG
dc.creatorRamos, Celso RR
dc.creatorOliveira, Carla C
dc.date.accessioned2013-08-26T17:10:53Z
dc.date.accessioned2018-07-04T16:28:54Z
dc.date.available2013-08-26T17:10:53Z
dc.date.available2018-07-04T16:28:54Z
dc.date.created2013-08-26T17:10:53Z
dc.date.issued2010
dc.identifier1756-0500
dc.identifierhttp://www.producao.usp.br/handle/BDPI/33169
dc.identifier10.1186/1756-0500-3-97
dc.identifierhttp://www.biomedcentral.com/1756-0500/3/97
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1636177
dc.description.abstractAbstract Background The gene coding for the uncharacterized protein PAB1135 in the archaeon Pyrococcus abyssi is in the same operon as the ribonuclease P (RNase P) subunit Rpp30. Findings Here we report the expression, purification and structural analysis of PAB1135. We analyzed the interaction of PAB1135 with RNA and show that it binds efficiently double-stranded RNAs in a non-sequence specific manner. We also performed molecular modeling of the PAB1135 structure using the crystal structure of the protein Af2318 from Archaeoglobus fulgidus (2OGK) as the template. Conclusions Comparison of this model has lead to the identification of a region in PAB1135 that could be involved in recognizing double-stranded RNA.
dc.languageeng
dc.relationBMC Research Notes
dc.rightsOliveira et al; licensee BioMed Central Ltd. - This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
dc.rightsopenAccess
dc.titleExpression, purification and structural analysis of the Pyrococcus abyssi RNA binding protein PAB1135
dc.typeArtículos de revistas


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