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Characterization of the RNase R association with ribosomes

BACKGROUND: In this study we employed the TAP tag purification method coupled with mass spectrometry analysis to identify proteins that co-purify with Escherichia coli RNase R during exponential growth and after temperature downshift. RESULTS: Our initial results suggested that RNase R can interact...

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Detalles Bibliográficos
Autores principales: Malecki, Michal, Bárria, Cátia, Arraiano, Cecilia M
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3942186/
https://www.ncbi.nlm.nih.gov/pubmed/24517631
http://dx.doi.org/10.1186/1471-2180-14-34
Descripción
Sumario:BACKGROUND: In this study we employed the TAP tag purification method coupled with mass spectrometry analysis to identify proteins that co-purify with Escherichia coli RNase R during exponential growth and after temperature downshift. RESULTS: Our initial results suggested that RNase R can interact with bacterial ribosomes. We subsequently confirmed this result using sucrose gradient ribosome profiling joined with western blot analysis. We found that RNase R co-migrates with the single 30S ribosomal subunits. Independent data involving RNase R in the rRNA quality control process allowed us to hypothesize that the RNase R connection with ribosomes has an important physiological role. CONCLUSIONS: This study leads us to conclude that RNase R can interact with ribosomal proteins and that this interaction may be a result of this enzyme involvement in the ribosome quality control.