PMID:9016593
| Citation |
Böddeker, N, Stade, K and Franceschi, F (1997) Characterization of DbpA, an Escherichia coli DEAD box protein with ATP independent RNA unwinding activity. Nucleic Acids Res. 25:537-45 |
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| Abstract |
DbpA is a putative Escherichia coli ATP dependent RNA helicase belonging to the family of DEAD box proteins. It hydrolyzes ATP in the presence of 23S ribosomal RNA and 93 bases in the peptidyl transferase center of 23S rRNA are sufficient to trigger 100% of the ATPase activity of DbpA. In the present study we characterized the ATPase and RNA unwinding activities of DbpA in more detail. We report that-in contrast to eIF-4A, the prototype of the DEAD box protein family-the ATPase and the helicase activities of DbpA are not coupled. Moreover, the RNA unwinding activity of DbpA is not specific for 23S rRNA, since DbpA is also able to unwind 16S rRNA hybrids. Furthermore, we determined that the ATPase activity of DbpA is triggered to a significant extent not only by the 93 bases of the 23S rRNA previously reported but also by other regions of the 23S rRNA molecule. Since all these regions of 23S rRNA are either part of the 'functional core' of the 50S ribosomal subunit or involved in the 50S assembly, DbpA may play an important role in the ribosomal assembly process. |
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| Keywords |
Adenosine Triphosphatases/genetics; Adenosine Triphosphatases/metabolism; Adenosine Triphosphate/metabolism; Amino Acid Sequence; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Base Sequence; DEAD-box RNA Helicases; DNA, Bacterial; Escherichia coli Proteins; Molecular Sequence Data; Nucleic Acid Conformation; Nucleic Acid Hybridization; RNA Helicases; RNA Nucleotidyltransferases/genetics; RNA Nucleotidyltransferases/metabolism; RNA, Ribosomal, 16S/metabolism; RNA, Ribosomal, 23S/metabolism; RNA, Ribosomal, 5S/metabolism; RNA-Binding Proteins/genetics; RNA-Binding Proteins/metabolism; Recombinant Fusion Proteins/genetics; Recombinant Fusion Proteins/metabolism |
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Useful Materials and Methods
To study which regions of the 23S rRNA stimulates DbpA's ATPase activity, the authors generated the RNA fragments using RNase H treatment instead of in vitro transcription. This helped avoid the risk of incorrect folding of the RNA.
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