Journal
NATURE
Volume 509, Issue 7502, Pages 588-+Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nature13271
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Funding
- Swiss National Science Foundation (SNF) [3100A0-118118, 31003ab-133134, 31003A-149921]
- SNF-NCCR structural biology Iso-lab
- Swiss National Science Foundation (SNF) [31003AB_133134, 31003A_149921] Funding Source: Swiss National Science Foundation (SNF)
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MicroRNA and protein sequestration by non-coding RNAs (ncRNAs) has recently generated much interest. In the bacterial Csr/Rsm system, which is considered to be the most general global post-transcriptional regulatory system responsible for bacterial virulence, ncRNAs such as CsrB or RsmZ activate translation initiation by sequestering homodimeric CsrA-type proteins from the ribosome-binding site of a subset of messenger RNAs. However, the mechanism of ncRNA-mediated protein sequestration is not understood at the molecular level. Here we show for Pseudomonas fluorescens that RsmE protein dimers assemble sequentially, specifically and cooperatively onto the ncRNA RsmZ within a narrow affinity range. This assembly yields two different native ribonucleoprotein structures. Using a powerful combination of nuclear magnetic resonance and electron paramagnetic resonance spectroscopy we elucidate these 70-kilodalton solution structures, thereby revealing the molecular mechanism of the sequestration process and how RsmE binding protects the ncRNA from RNase E degradation. Overall, our findings suggest that RsmZ is well-tuned to sequester, store and release RsmE and therefore can be viewed as an ideal protein 'sponge'.
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