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Updated: Jun 14, 2026

Novel RNA-Binding Proteins Isolation by the RaPID Methodology
Published on: September 30, 2016
Expression, purification and structural analysis of the Pyrococcus abyssi RNA binding protein PAB1135
Juliana S Luz1, João Arg Barbosa, Celso Rr Ramos
1Department of Biochemistry, Institute of Chemistry, University of São Paulo, 05508-000, São Paulo, SP, Brazil. ccoliv@iq.usp.br.
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.
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