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

Juliana S Luz1, João ARG Barbosa23, Celso RR Ramos14 and Carla C Oliveira1*

Author Affiliations

1 Department of Biochemistry, Institute of Chemistry, University of São Paulo, 05508-000, São Paulo, SP, Brazil

2 Center for Structural Molecular Biology, Brazilian Synchrotron Light Laboratory, LNLS, 13083-970, Campinas, SP, Brazil

3 Current address: Pós-Graduação em Ciências Genômicas e Biotecnologia, Universidade Católica de Brasília, 70790-160, Brasília, DF, Brazil

4 Current address: Department of Helminthology, Fiocruz, 21045-900, Rio de Janeiro, RJ, Brazil

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BMC Research Notes 2010, 3:97  doi:10.1186/1756-0500-3-97

Published: 9 April 2010

Abstract

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.