Article: article from journal or magazin.
Molecular basis of messenger RNA recognition by the specific bacterial repressing clamp RsmA/CsrA.
Nature Structural and Molecular Biology
Proteins of the RsmA/CsrA family are global translational regulators in many bacterial species. We have determined the solution structure of a complex formed between the RsmE protein, a member of this family from Pseudomonas fluorescens, and a target RNA encompassing the ribosome-binding site of the hcnA gene. The RsmE homodimer with its two RNA-binding sites makes optimal contact with an 5'-A/UCANGGANGU/A-3' sequence in the mRNA. When tightly gripped by RsmE, the ANGGAN core folds into a loop, favoring the formation of a 3-base-pair stem by flanking nucleotides. We validated these findings by in vivo and in vitro mutational analyses. The structure of the complex explains well how, by sequestering the Shine-Dalgarno sequence, the RsmA/CsrA proteins repress translation.
Amino Acid Sequence, Bacterial Proteins/chemistry, Bacterial Proteins/metabolism, Electrophoretic Mobility Shift Assay, Models, Molecular, Molecular Sequence Data, Nuclear Magnetic Resonance, Biomolecular, Pseudomonas aeruginosa/metabolism, RNA, Bacterial/metabolism, RNA, Messenger/genetics, RNA, Messenger/metabolism, RNA-Binding Proteins/chemistry, RNA-Binding Proteins/metabolism
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