Structural and energetic analysis of RNA recognition by a universally conserved protein from the signal recognition particle
Copyright policy )Structural and energetic analysis of RNA recognition by a universally conserved protein from the signal recognition particle
The signal recognition particle (SRP) is a ribonucleoprotein complex responsible for targeting proteins to the endoplasmic reticulum in eukarya or to the inner membrane in prokarya. The crystal structure of the universally conserved RNA-protein core of the Escherichia coli SRP, refined here to 1.5 A resolution, revealed minor groove recognition of the 4.5 S RNA component by the M domain of the Ffh protein. Within the RNA, nucleotides comprising two phylogenetically conserved internal loops create a unique surface for protein recognition. To determine the energetic importance of conserved nucleotides for SRP assembly, we measured the affinity of the M domain for a series of RNA mutants. This analysis reveals how conserved nucleotides within the two internal loop motifs establish the architecture of the macromolecular interface and position essential functional groups for direct recognition by the protein.
- Howard Hughes Medical Institute United States
- Yale University United States
Models, Molecular, Protein Conformation, RNA-Binding Proteins, Crystallography, X-Ray, Protein Structure, Tertiary, RNA, Bacterial, RNA, Ribosomal, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Escherichia coli, Humans, Nucleic Acid Conformation, Crystallization, Signal Recognition Particle, Conserved Sequence
Models, Molecular, Protein Conformation, RNA-Binding Proteins, Crystallography, X-Ray, Protein Structure, Tertiary, RNA, Bacterial, RNA, Ribosomal, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Escherichia coli, Humans, Nucleic Acid Conformation, Crystallization, Signal Recognition Particle, Conserved Sequence
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