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Journal ArticleDOI

Resolution of two factors required in the Q-beta-RNA polymerase reaction.

Lucille Shapiro, +2 more
- 02 Nov 1968 - 
- Vol. 220, Iss: 5166, pp 478-480
TLDR
The results suggest that the role of factor is to promote a step in the reaction occurring after association of the enzyme with Qβ-RNA, but before nucleotide polymerization.
Abstract
THE Escherichia coli bacteriophage Qβ contains RNA as its genetic component. Qβ-RNA can be synthesized in vitro in the reaction catalysed by the Qβ-RNA polymerase isolated from Qβ infected E. coli1. The synthesis of infectious Qβ-RNA requires, in addition to the polymerase, the phage RNA to serve as template, ribonucleoside tri-phosphate substrates, Mg++, and a factor fraction obtained from both infected and uninfected E. coli2. Previous studies with the factor have suggested that it acts on Qβ-RNA at some early step in the reaction2. Although an association of the enzyme and Qβ-RNA occurs in the absence of this factor3, synthesis of the complementary minus strand is not detected. The requirement for this agent in the reaction seems to bear a quantitative relationship to Qβ-RNA but not to enzyme2. The factor fraction, furthermore, is not required for enzyme activity when synthetic polymers4, minus strands or other RNA molecules3 are used as template. These results suggest that the role of factor is to promote a step in the reaction occurring after association of the enzyme with Qβ-RNA, but before nucleotide polymerization.

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Citations
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Journal ArticleDOI

Hfq Is Necessary for Regulation by the Untranslated RNA DsrA

TL;DR: It is shown that an hfq mutant strain is defective for DsrA-mediated regulation of both rpoS and hns, and Hfq acts as a protein cofactor for the regulatory activities of D srA by either altering the structure of DSRA or forming an active RNA-protein complex.
Book ChapterDOI

Alfalfa mosaic virus

TL;DR: This chapter is intended to bring together information on a wide range of topics and to offer some possible explanations of the unusual in vivo and in vitro behavior of this virus.
Journal ArticleDOI

Bacterial proteins required for replication of phage Q ribonucleic acid. Pruification and properties of host factor I, a ribonucleic acid-binding protein.

TL;DR: A bacterial protein required for the replication of bacteriophage Qβ RNA in vitro has been purified from uninfected Escherichia coli to apparent homogeneity and studies on the role of factor suggest that this host protein acts as a positive control element required at some step prior to the initiation of synthesis with Q β RNA template.
Journal ArticleDOI

Characterization of the subunits of Q-beta replicase.

TL;DR: The RNA replicating enzyme induced by RNA phage Qβ consists of a single phage specific and three host specific polypeptide chains, and none are known subunits of E. coli DNA-dependent RNA polymerase.
Journal ArticleDOI

Regulation of the Escherichia coli hfq gene encoding the host factor for phage Q beta.

TL;DR: The host factor for phage Q beta RNA replication is a small protein of 102 amino acid residues encoded by the hfq gene at 94.8 min on the Escherichia coli chromosome, and it is suggested that HF-I is one of the growth-related proteins.
References
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Journal ArticleDOI

Factor Fraction required for the Synthesis of Bacteriophage Qβ-RNA

TL;DR: A factor fraction essential for the in vitro synthesis of RNA bacteriophage Qβ-RNA has been isolated from both infected and uninfected E. coli and indicates that the contribution of the last bacterium to the replication of Q β-RNA is more extensive than was earlier thought.
Journal ArticleDOI

Replication of RNA viruses. V. Template activity of synthetic ribopolymers in the Q-beta RNA polymerase reaction.

TL;DR: With the discovery that the Qf RNA polymerase will utilize certain synthetic polynucleotides as template, the specificity of template function with synthetic polymers appears to be related to the initiation of synthesis with GTP.
Journal ArticleDOI

Comparison of RNA Terminal Sequences of Phages f2 and Qβ: Chemical and Sedimentation Equilibrium Studies

TL;DR: The terminal fragment obtained by hydrolysis with ribonuclease T1 of the ribonucleic acid from the bacteriophage Qβ has been isolated and purified and indicates that the fragment has the composition (10 Cp, 4 Up), and that the RNA has the terminal sequence -GP(9 Cp), 4 Up) CpA.
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