Abstract
The ring-shaped RNA chaperone Hfq has recently received much attention owing to its multiple roles in RNA metabolism. In this study we have performed a mutational analysis of the Escherichia coli hfq gene, and have studied the effects of amino acid substitutions at several positions in the Hfq protein as well as of C-terminal truncations on its role in phage Qbeta replication, in repression of a target mRNA, and on the stability of the small regulatory RNA DsrA. These functional studies provided insights into the interaction of Hfq with RNA and suggested a role for the C-terminus of Hfq in DsrA stability.
Publication types
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Comparative Study
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Evaluation Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Allolevivirus / growth & development
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Amino Acid Substitution
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Bacterial Outer Membrane Proteins / genetics
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Bacterial Outer Membrane Proteins / metabolism*
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Escherichia coli / genetics
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Escherichia coli / metabolism*
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Escherichia coli / virology
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Escherichia coli Proteins / genetics*
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Escherichia coli Proteins / metabolism*
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Host Factor 1 Protein / genetics*
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Host Factor 1 Protein / metabolism*
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Molecular Chaperones / genetics
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Molecular Chaperones / metabolism*
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Mutagenesis, Site-Directed
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RNA / genetics*
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RNA / metabolism*
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RNA, Small Untranslated
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RNA, Untranslated / genetics
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RNA, Untranslated / metabolism
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Recombinant Proteins / metabolism
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Structure-Activity Relationship
Substances
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Bacterial Outer Membrane Proteins
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DrsA protein, E coli
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DsrA RNA, E coli
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Escherichia coli Proteins
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Hfq protein, E coli
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Host Factor 1 Protein
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Molecular Chaperones
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RNA, Small Untranslated
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RNA, Untranslated
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Recombinant Proteins
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OMPA outer membrane proteins
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RNA