Download full-text PDF |
Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC224554 | PMC |
| http://dx.doi.org/10.1073/pnas.57.6.1833 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Probing RNA-protein interactions using pyrene-labeled oligodeoxynucleotides: Qbeta replicase efficiently binds small RNAs by recognizing pyrimidine residues.
J Mol Biol
October 1997
Department of Biochemical Kinetics, Max-Planck-Institute for Biophysical Chemistry, Am Fassberg, Göttingen, D-37077, Germany.
Binding of small RNAs by the RNA-dependent RNA polymerase of coliphage Qbeta was studied utilizing a fluorometric assay. A DNA oligonucleotide probe of sequence 5'-d(TTTTTCC) was 5'-end-labeled with pyrene. In this construct, the proximal thymine residues efficiently quench the fluorophore emission in solution.
View Article and Find Full Text PDFTemplate recognition by an RNA-dependent RNA polymerase: identification and characterization of two RNA binding sites on Q beta replicase.
Biochemistry
November 1995
Department of Molecular, Cellular and Developmental Biology, University of Colorado at Boulder 80309-0347, USA.
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.
View Article and Find Full Text PDFStability of replicative form and fitness among RNA variants transcribed by Qbeta replicase.
Proc Biol Sci
April 1995
Research Foundation of Southern California, La Jolla 92037, USA.
Stability in the replicative form of RNA molecules transcribed by Qbeta replicase was demonstrated to provide a sequence-dependent indicator of their fitness. This follows from the finding that replication rates reported for 17 RNA species (genome length, 77-370 nucleotides) correlate with the self-interaction free energy of these self-annealed strands. Formation of double-stranded molecules during replication conversely decreased with self-interaction free energy.
View Article and Find Full Text PDFKinetic and thermodynamic characterization of the interaction between Q beta-replicase and template RNA molecules.
Biochemistry
June 1991
Max-Planck-Institut für Biophysikalische Chemie, Göttingen, Federal Republic of Germany.
The specific binding of the RNA polymerase Q beta-replicase to some of its RNA template molecules, the single-stranded RNA variant MDV and also Q beta-RNA, was studied under various conditions by using a gel-retardation assay as well as filter retention. The dissociation of the replicase-RNA complex proceeds with first-order kinetics. The dependence of the dissociation rate constant on the concentration of monovalent ions suggests that there are three contacts between the midivariant (MDV) RNA and the replicase.
View Article and Find Full Text PDFWe observed the secondary structures that formed in an RNA molecule during its synthesis. Some of the secondary structures seen in nascent chains were observed to form, then to dissociate in favor of an alternative structure, and then to reform, as chain growth continued. The results show that secondary structures in an RNA molecule are in a state of dynamic equilibrium, and that the extension of a sequence by chain growth, or the reduction of a sequence by processing, may result in significant changes in the secondary structures that are present.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!