Journal
BMC MICROBIOLOGY
Volume 14, Issue -, Pages -Publisher
BIOMED CENTRAL LTD
DOI: 10.1186/1471-2180-14-34
Keywords
Ribonucleases; RNA; Ribosomes; RNase R
Categories
Funding
- Fundacao para a Clencia e a Tecnologia (FCT), Portugal [Pest-OE/EQB/LA0004/2011, PTDC/BIQ/111757/2009, PTDC/BIA-MIC/4142/2012, FP7-KBBE-2011-1-289326]
- Marie Curie Individual European Fellowship [PIEF-GA-2009-254183]
- FCT
- Fundação para a Ciência e a Tecnologia [PTDC/BIA-MIC/4142/2012] Funding Source: FCT
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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.
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