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Template recognition by an RNA-dependent ... nding sites on Q beta replicase
Template recognition by an RNA-dependent RNA polymerase: identification and characterization of two RNA binding sites on Q beta replicase.
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Two different SELEX protocols were used to generate two classes of RNA ligands that bound Q beta replicase with nanomolar equilibrium dissociation constants. One set of RNAs appeared to exist as pseudoknots with conserved loop sequences. These ligands bound Q beta replicase and ribosomal protein S1 with equal affinities, indicating that the RNAs bind the replicase through its S1 subunit. The second class of ligands bound the replicase via a pyrimidine rich region. The two sets of ligands did not compete for binding to Q beta replicase, demonstrating that the two RNA families bind unique sites on the phage polymerase. Because the second class of ligands bound ribosomal protein S1 very poorly, it is likely that the second RNA binding site is located on one of the three remaining replicase subunits. Published sequences of RNAs replicated by Q beta replicase possess similarities to the two classes of RNA ligands, providing a possible solution to the question of template recognition by the phage polymerase.
Brown D, Gold L
Biochemistry
1995-11-14 00:00
34
45
14765-74
Aspergillus Nuclease S1,Base Composition,Base Sequence,Binding Sites,DNA Primers,Molecular Sequence Data,Nucleic Acid Conformation,Oligoribonucleotides,Polymerase Chain Reaction,Q beta Replicase,RNA,DNA Primers,Oligoribonucleotides,RNA,Q beta Replicase,Aspergillus Nuclease S1
Department of Molecular, Cellular and Developmental Biology, University of Colorado at Boulder 80309-0347, USA
Biochemistry
NIGMS GM19963, NIGMS GM28685
0006-2960
445
True
7578085
