title: Molecular basis of messenger RNA recognition by the specific bacterial repressing clamp RsmA/CsrA.
abstract: 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.
authors: Institute of Molecular Biology and Biophysics, ETH Zürich, CH-8093 Zürich, Switzerland.
authors: Mario
authors: M
authors: Schubert
authors: Karine
authors: K
authors: Lapouge
authors: Olivier
authors: O
authors: Duss
authors: Florian C
authors: FC
authors: Oberstrass
authors: Ilian
authors: I
authors: Jelesarov
authors: Dieter
authors: D
authors: Haas
authors: Frédéric H-T
authors: FH
authors: Allain
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism / Q000502:physiology*; D024202:Electrophoretic Mobility Shift Assay; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D011550:Pseudomonas aeruginosa / Q000378:metabolism*; D012329:RNA, Bacterial / Q000378:metabolism; D012333:RNA, Messenger / Q000235:genetics / Q000378:metabolism*; D016601:RNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism / Q000502:physiology*
chemical_list: D001426:Bacterial Proteins; D012329:RNA, Bacterial; D012333:RNA, Messenger; D016601:RNA-Binding Proteins