Nucleic Acids Research, Vol 25, Issue 3 537-545, Copyright © 1997 by Oxford University Press
N Boddeker, K Stade and F Franceschi
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.
ARTICLES
Characterization of DbpA, an Escherichia coli DEAD box protein with ATP independent RNA unwinding activity
Max-Planck-Institut fur Molekulare Genetik, AG Ribosomen, Ihnestrasse 73, 14195 Berlin, Germany.
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