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

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Year: 1992, Volume: 1, Issue: 6

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

Content Provider	PubMed Central
Author	Geiselmann, J. Yager, T. D. Hippel, P. H. Von
Abstract	The rho protein of Escherichia coli interacts with the nascent RNA transcript while RNA polymerase is paused at specific rho-dependent termination sites on the DNA template, and (in a series of steps that are still largely undefined) brings about transcript termination at these sites. In this paper we characterize the interactions of rho with RNA and relate these interactions to the quaternary structure of the functional form of rho. We use CD spectroscopy and analytical ultracentrifugation to determine the binding interactions of rho with RNA ligands of defined length ([rC]n where n > or = 6). Rho binds to long RNA chains as a hexamer characterized by D3 symmetry. Each hexamer binds approximately 70 residues of RNA. We show by ultracentrifugation and dynamic laser light scattering that, in the presence of RNA ligands less than 22 nucleotide residues in length, rho changes its quaternary structure and becomes a homogeneous dodecamer. The dodecamer contains six strong binding sites for short RNA ligands: i.e., one site for every two rho protomers. The measured association constant of these short RNAs to rho increases with increasing (rC)n length, up to n = 9, suggesting that the binding site of each rho protomer interacts with 9 RNA nucleotide residues. Oligo (rC) ligands bound to the strong RNA binding sites on the rho dodecamer do not significantly stimulate the RNA-dependent ATPase activity of rho. Based on these features of the rho-RNA interaction and other experimental data we propose a molecular model of the interaction of rho with its cofactors.
Related Links	http://dx.doi.org/10.1002/pro.5560010704
Ending Page	873
Page Count	13
Starting Page	861
File Format	PDF
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science : A Publication of the Protein Society
Issue Number	7
Volume Number	1
Language	English
Publisher	Cold Spring Harbor Laboratory Press
Publisher Date	1992-07-01
Access Restriction	Open
Rights Holder	Cold Spring Harbor Laboratory Press
Subject Keyword	Biochemistry Molecular Biology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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Functional interactions of ligand cofactors with Escherichia coli transcription termination factor rho. I. Binding of ATP.

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

Functional interactions of ligand cofactors with Escherichia coli transcription termination factor rho. I. Binding of ATP.

Escherichia coli transcription termination factor rho. II. Binding of oligonucleotide cofactors.

Sequence-specific Interactions in the RNA-binding Domain of Escherichia coli Transcription Termination Factor Rho

Escherichia coli transcription termination factor rho. I. ATPase activation by oligonucleotide cofactors.

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Transcription Elongation Factor NusA Is a General Antagonist of Rho-dependent Termination in Escherichia coli

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

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