Abstract
The signal recognition particle (SRP), a protein-RNA complex conserved in all three kingdoms of life, recognizes and transports specific proteins to cellular membranes for insertion or secretion. We describe here the 1.8 angstrom crystal structure of the universal core of the SRP, revealing protein recognition of a distorted RNA minor groove. Nucleotide analog interference mapping demonstrates the biological importance of observed interactions, and genetic results show that this core is functional in vivo. The structure explains why the conserved residues in the protein and RNA are required for SRP assembly and defines a signal sequence recognition surface composed of both protein and RNA.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
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Comment
MeSH terms
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Amino Acid Sequence
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Bacterial Proteins / chemistry*
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Bacterial Proteins / metabolism
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Base Pairing
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Binding Sites
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Cell Membrane / metabolism
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Crystallography, X-Ray
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Escherichia coli / chemistry
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Escherichia coli / genetics
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Escherichia coli / metabolism
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Escherichia coli Proteins*
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Guanosine Triphosphate / metabolism
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Hydrogen Bonding
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Magnesium / metabolism
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Models, Molecular
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Molecular Sequence Data
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Nucleic Acid Conformation
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Potassium / metabolism
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Protein Binding
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Protein Conformation
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Protein Structure, Secondary
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Protein Structure, Tertiary
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RNA, Bacterial / chemistry*
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RNA, Bacterial / genetics
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RNA, Bacterial / metabolism
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Signal Recognition Particle / chemistry*
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Signal Recognition Particle / metabolism
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Transformation, Bacterial
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Water / metabolism
Substances
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Bacterial Proteins
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Escherichia coli Proteins
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Ffh protein, E coli
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RNA, Bacterial
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Signal Recognition Particle
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Water
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Guanosine Triphosphate
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Magnesium
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Potassium