Structural Rearrangement in an RsmA/CsrA Ortholog of Pseudomonas aeruginosa Creates a Dimeric RNA-Binding Protein, RsmN
| Autor: | Mark S. Searle, Paul Williams, Elizabeth R. Morris, Chan Li, Rahul V. Kulkarni, Marco Messina, Gareth Hall, Miguel Cámara, Hazel Silistre, Laura Lovelock, Jonas Emsley, Stephan Heeb |
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| Jazyk: | angličtina |
| Předmět: |
Models
Molecular Molecular Sequence Data Mutant Beta sheet RNA-binding protein Biology Crystallography X-Ray Article Protein Structure Secondary Bacterial Proteins Structural Biology Amino Acid Sequence Molecular Biology Gene Genetics Binding Sites Base Sequence Inverted Repeat Sequences RNA-Binding Proteins RNA Hydrogen Bonding Protein superfamily Protein Structure Tertiary Complementation RNA Bacterial Pseudomonas aeruginosa Transfer RNA Hydrophobic and Hydrophilic Interactions Protein Binding |
| Zdroj: | Structure(London, England:1993) |
| ISSN: | 0969-2126 |
| DOI: | 10.1016/j.str.2013.07.007 |
| Popis: | Summary In bacteria, the highly conserved RsmA/CsrA family of RNA-binding proteins functions as global posttranscriptional regulators acting on mRNA translation and stability. Through phenotypic complementation of an rsmA mutant in Pseudomonas aeruginosa, we discovered a family member, termed RsmN. Elucidation of the RsmN crystal structure and that of the complex with a hairpin from the sRNA, RsmZ, reveals a uniquely inserted α helix, which redirects the polypeptide chain to form a distinctly different protein fold to the domain-swapped dimeric structure of RsmA homologs. The overall β sheet structure required for RNA recognition is, however, preserved with compensatory sequence and structure differences, allowing the RsmN dimer to target binding motifs in both structured hairpin loops and flexible disordered RNAs. Phylogenetic analysis indicates that, although RsmN appears unique to P. aeruginosa, homologous proteins with the inserted α helix are more widespread and arose as a consequence of a gene duplication event. Highlights • Phenotypic complementation identifies a CsrA/RsmA family member from P. aeruginosa • Crystallography reveals a dimeric fold for RsmN • The RsmN complex was solved with a hairpin motif from the noncoding sRNA RsmZ-2 • Details of binding affinity and specificity with target RNA 5′-ANGGAN motifs are revealed The RsmA/CsrA family of bacterial RNA-binding proteins functions as global posttranscriptional regulators of mRNA. Morris et al. discover an additional family member in P. aeruginosa, RsmN. The structure of an RsmN/RNA complex reveals a unique protein fold and molecular details of base-specific RNA recognition. |
| Databáze: | OpenAIRE |
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