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

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.

SUBMITTER: Luz JS

PROVIDER: S-EPMC2872656 | biostudies-literature | 2010

REPOSITORIES: biostudies-literature

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

Luz Juliana S JS Barbosa João Arg JA Ramos Celso Rr CR Oliveira Carla C CC

BMC research notes 20100409

<h4>Background</h4>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.<h4>Findings</h4>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 structu ...[more]

PMID: 20380716

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