Literature DB >> 138682

Characterization of the nucleoside triphosphate phosphohydrolase (ATPase) activity of RNA synthesis termination factor p. II. Influence of synthetic RNA homopolymers and random copolymers on the reaction.

C Lowery, J P Richardson.   

Abstract

The ability of various kinds of RNA molecules to activate the ATP hydrolysis reaction catalyzed by the p transcription termination factor from Escherichia coli has been studied. The most active RNA polymers are those containing cytidylate residues and very little ordered structure. Free poly(C) is the most active homopolymer; it is 45 times more active than poly(U), which is the only non-cytidine containing RNA that has detectable activity. Poly(C) has no activity when complexed with poly(I) or when the chain lengths are shorter than 22 nucleotides long. Although cytidylate residues are important they need not be frequent; a random copolymer of uridine and cytidine nucleotides with as few as 1 cytidylate residue out of 20 is as active as poly(C). The extent of activation with poly(C) depends on the ratio of p to poly(C). Poly(C) becomes saturated with p at a ratio of 1.8 ng of p/pmol poly(C), which is equivalent to one p monomer/27 nucleotides. A further increase in this ratio leads to a reduction in p activity. Decreasing the length of the poly(C) does not alter the observed saturation value but does decrease the rate of ATP hydrolysis when the RNA is in excess. The possible relevance of these results to p termination activity is discussed.

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Year:  1977        PMID: 138682

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  20 in total

1.  Functional interactions of ligand cofactors with Escherichia coli transcription termination factor rho. II. Binding of RNA.

Authors:  J Geiselmann; T D Yager; P H von Hippel
Journal:  Protein Sci       Date:  1992-07       Impact factor: 6.725

2.  ATPase activity of transcription-termination factor rho: functional dimer model.

Authors:  S E Seifried; J B Easton; P H von Hippel
Journal:  Proc Natl Acad Sci U S A       Date:  1992-11-01       Impact factor: 11.205

3.  Cell-free translation of purified virion-associated high-molecular-weight RNA synthesized in vitro by vaccinia virus.

Authors:  W Bossart; E Paoletti; D L Nuss
Journal:  J Virol       Date:  1978-12       Impact factor: 5.103

4.  A physical model for the translocation and helicase activities of Escherichia coli transcription termination protein Rho.

Authors:  J Geiselmann; Y Wang; S E Seifried; P H von Hippel
Journal:  Proc Natl Acad Sci U S A       Date:  1993-08-15       Impact factor: 11.205

5.  Escherichia coli transcription termination factor rho has a two-domain structure in its activated form.

Authors:  D G Bear; C L Andrews; J D Singer; W D Morgan; R A Grant; P H von Hippel; T Platt
Journal:  Proc Natl Acad Sci U S A       Date:  1985-04       Impact factor: 11.205

6.  RNA sequence containing hexanucleotide AAUAAA directs efficient mRNA polyadenylation in vitro.

Authors:  J L Manley; H Yu; L Ryner
Journal:  Mol Cell Biol       Date:  1985-02       Impact factor: 4.272

Review 7.  Processive Antitermination.

Authors:  Jonathan R Goodson; Wade C Winkler
Journal:  Microbiol Spectr       Date:  2018-09

8.  A mutant rho ATPase from Escherichia coli that is temperature-sensitive in the presence of RNA.

Authors:  R B Kent; S K Guterman
Journal:  Mol Gen Genet       Date:  1981

9.  Pyrophosphate inhibition of rho ATPase: a mechanism of coupling to RNA polymerase activity.

Authors:  R B Kent; S K Guterman
Journal:  Proc Natl Acad Sci U S A       Date:  1982-07       Impact factor: 11.205

10.  The attenuator of the tryptophan operon in E.coli: rho-mediated release of RNA polymerase from a transcription termination complex in vitro.

Authors:  R S Fuller; T Platt
Journal:  Nucleic Acids Res       Date:  1978-12       Impact factor: 16.971

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