PMID:14654705
| Citation |
Folichon, M, Arluison, V, Pellegrini, O, Huntzinger, E, Régnier, P and Hajnsdorf, E (2003) The poly(A) binding protein Hfq protects RNA from RNase E and exoribonucleolytic degradation. Nucleic Acids Res. 31:7302-10 |
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| Abstract |
The Hfq protein, which shares sequence and structural homology with the Sm and Lsm proteins, binds to various RNAs, primarily recognizing AU-rich single-stranded regions. In this paper, we study the ability of the Escherichia coli Hfq protein to bind to a polyadenylated fragment of rpsO mRNA. Hfq exhibits a high specificity for a 100-nucleotide RNA harboring 18 3'-terminal A-residues. Structural analysis of the adenylated RNA-Hfq complex and gel shift assays revealed the presence of two Hfq binding sites. Hfq binds primarily to the poly(A) tail, and to a lesser extent a U-rich sequence in a single-stranded region located between two hairpin structures. The oligo(A) tail and the interhelical region are sensitive to 3'-5' exoribonucleases and RNase E hydrolysis, respectively, in vivo. In vitro assays demonstrate that Hfq protects poly(A) tails from exonucleolytic degradation by both PNPase and RNase II. In addition, RNase E processing, which occurred close to the U-rich sequence, is impaired by the presence of Hfq. These data suggest that Hfq modulates the sensitivity of RNA to ribonucleases in the cell. |
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| Keywords |
Base Sequence; Binding Sites; Electrophoretic Mobility Shift Assay; Endoribonucleases/metabolism; Escherichia coli Proteins/metabolism; Exoribonucleases/metabolism; Host Factor 1 Protein/metabolism; Molecular Sequence Data; Nucleic Acid Conformation; Poly A/chemistry; Poly A/genetics; Poly A/metabolism; Polyribonucleotide Nucleotidyltransferase/metabolism; RNA Processing, Post-Transcriptional; RNA, Messenger/chemistry; RNA, Messenger/genetics; RNA, Messenger/metabolism; Ribosomal Proteins/genetics; Substrate Specificity; Thermodynamics |
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