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

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...

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Detalles Bibliográficos
Autores principales: Luz, Juliana S, Barbosa, João ARG, Ramos, Celso RR, Oliveira, Carla C
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2010
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2872656/
https://www.ncbi.nlm.nih.gov/pubmed/20380716
http://dx.doi.org/10.1186/1756-0500-3-97
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author Luz, Juliana S
Barbosa, João ARG
Ramos, Celso RR
Oliveira, Carla C
author_facet Luz, Juliana S
Barbosa, João ARG
Ramos, Celso RR
Oliveira, Carla C
author_sort Luz, Juliana S
collection PubMed
description 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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spelling pubmed-28726562010-05-19 Expression, purification and structural analysis of the Pyrococcus abyssi RNA binding protein PAB1135 Luz, Juliana S Barbosa, João ARG Ramos, Celso RR Oliveira, Carla C BMC Res Notes Short Report 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. BioMed Central 2010-04-09 /pmc/articles/PMC2872656/ /pubmed/20380716 http://dx.doi.org/10.1186/1756-0500-3-97 Text en Copyright ©2010 Oliveira et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 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.
spellingShingle Short Report
Luz, Juliana S
Barbosa, João ARG
Ramos, Celso RR
Oliveira, Carla C
Expression, purification and structural analysis of the Pyrococcus abyssi RNA binding protein PAB1135
title Expression, purification and structural analysis of the Pyrococcus abyssi RNA binding protein PAB1135
title_full Expression, purification and structural analysis of the Pyrococcus abyssi RNA binding protein PAB1135
title_fullStr Expression, purification and structural analysis of the Pyrococcus abyssi RNA binding protein PAB1135
title_full_unstemmed Expression, purification and structural analysis of the Pyrococcus abyssi RNA binding protein PAB1135
title_short Expression, purification and structural analysis of the Pyrococcus abyssi RNA binding protein PAB1135
title_sort expression, purification and structural analysis of the pyrococcus abyssi rna binding protein pab1135
topic Short Report
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2872656/
https://www.ncbi.nlm.nih.gov/pubmed/20380716
http://dx.doi.org/10.1186/1756-0500-3-97
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