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Science 5 January 2001: Vol. 291. no. 5501, pp. 121 - 125 DOI: 10.1126/science.291.5501.121
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Reports
Active Disruption of an RNA-Protein Interaction by a DExH/D RNA Helicase
Eckhard Jankowsky,1
Christian H. Gross,2
Stewart Shuman,2
Anna Marie Pyle13*
All aspects of cellular RNA metabolism and the replication of many
viruses require DExH/D proteins that manipulate RNA in a manner that
requires nucleoside triphosphates. Although DExH/D proteins have been
shown to unwind purified RNA duplexes, most RNA molecules in the
cellular environment are complexed with proteins. It has therefore been
speculated that DExH/D proteins may also affect RNA-protein
interactions. We demonstrate that the DExH protein NPH-II from vaccinia
virus can displace the protein U1A from RNA in an active adenosine
triphosphate-dependent fashion. NPH-II increases the
rate of U1A dissociation by more than three orders of magnitude while
retaining helicase processivity. This indicates that DExH/D proteins
can effectively catalyze protein displacement from RNA and thereby
participate in the structural reorganization of ribonucleoprotein
assemblies.
1 Department of Biochemistry and Molecular Biophysics,
Columbia University, New York, NY 10032, USA.
2 Sloan
Kettering Institute, New York, NY 10021, USA.
3 Howard
Hughes Medical Institute, Boston, MA 02115, USA.
*
To whom correspondence should be addressed. E-mail:
amp11{at}columbia.edu
Read the Full Text
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