Structural and functional properties of the segments of λ cro mRNA that interact with transcription termination factor Rho

Faus, Ignacio; Richardson, John P.

doi:10.1016/0022-2836(90)90304-5

Cited by 42 publications

(32 citation statements)

References 28 publications

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“…Tethered tracking models involve some form of tracking combined with continued binding of Rho to the initial loading site. Experimental support for such models includes the observation that this RNA sequence seems to be most protected in footprinting experiments on ATP-activated Rho-RNA complexes (45). In tracking models such as that described here, Rho is expected to scan and release each RNA chain repeatedly in the course of an experiment.…”

Section: Discussionmentioning

confidence: 90%

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

Geiselmann

Wang

Seifried

et al. 1993

Proc. Natl. Acad. Sci. U.S.A.

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Transcription 3' movement of the protein along the nascent RNA to elongation complexes paused at specific Rho-dependent termination sites on the DNA template. Rho then engages its ATPase-dependent RNA-DNA helicase activity to release the RNA from the transcription complex (5). The sequence specificity of Rho-dependent termination sites appears to reflect the extended dwell-time of the elongation complex at these positions (14-16). This extensive pausing allows Rho proteins that are translocating along the nascent RNA to "catch up" with the transcription complex at these sites, with the resultant termination efficiency depending on the "kinetic coupling" ofthe rate ofmovement ofRho along the nascent transcript and of RNA polymerase along the DNA template (1,17,18).The development of this view of Rho function has been paralleled by progress in elucidating its structural and enzymatic properties. It has been shown that Rho exists under physiological conditions as a hexamer of identical subunits (19-23), organized as a trimer of asymmetric dimers with overall D3 symmetry (24). This symmetry is reflected functionally in the presence of three strong and three weak ATP (substrate) and three strong and three weak RNA (cofactor) binding sites per Rho hexamer (25)(26)(27)(28) (37,38), and subunit interaction sites have been proposed in the C-terminal region (35). Rho monomers associate to form a hexamer with D3 symmetry under physiological conditions.

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Section: Discussionmentioning

confidence: 90%

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

Geiselmann

Wang

Seifried

et al. 1993

Proc. Natl. Acad. Sci. U.S.A.

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“…The N-dependent binding of antitermination factors to the nut site RNA probably reflects one mechanism by which N prevents transcription termination. The termination factor Rho binds to an RNA site called rutA, which overlaps the boxA component of nutR and enhances the action of Rho at the tR1 terminator (Bektesh and Richardson 1980;Lau and Roberts 1985;Faus and Richardson 1990). We did not use Rho in our experiments and therefore have shown here that Rho is not necessary for the association of antitermination factors with nut site RNA, but the N-dependent binding of antitermination factors to boxA may prevent the binding of Rho to rutA and, hence, lower the activity of tR1.…”

Section: Discussionmentioning

confidence: 99%

The nut site of bacteriophage lambda is made of RNA and is bound by transcription antitermination factors on the surface of RNA polymerase.

Nodwell¹,

Greenblatt²

1991

Genes Dev.

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The boxA and boxB components of the k nut site are important for transcriptional antitermination by the phage N protein. We show here that boxA and boxB RNA in N-modified transcription complexes are inaccessible to ribonucleases and have altered sensitivity to dimethylsulfate. N and NusA suffice to weakly protect boxB, independently of boxA and other factors. However, efficient protection of the entire nut site from ribonucleases requires boxA and boxB, N, NusA, NusB, Sl0, and NusG. Mutations in RNA polymerase, which inhibit antitermination by N in vivo, disallow protection of the nut site during transcription in vitro; therefore, the surface of RNA polymerase must coordinate the formation of complexes containing the antitermination factors and nut site RNA.

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“…The notion that Rho undergoes directed motion away from its initial binding site went unchallenged until the observation of a persistant Rho-RNA contact during ATP hydrolysis (Faus and Richardson, 1990). This suggested a 'tethered tracking' mechanism ( Fig.…”

Section: The Tethered Traddng Modelmentioning

confidence: 99%

Rho and RNA: models for recognition and response

Platt

1994

Molecular Microbiology

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SummaryEscherichia coli Rho factor Is required for termination of transcription at certain sites by RNA potymerase. Binding to unstructured cytosine^ontaining RNA target sites, subsequent RNA-dependent ATP hydrolysis, and an RNA-DNA helicase activity that presumably facilitates termination, are considered essential for Rho function. Yet the RNA recognition elements have remained elusive, the parameters relating RNA binding to ATPase activation have been obscure, and the mechanistic steps that integrate Rho's characteristics with its termination function in vitro and in vivo have been iargely undefined. Recent work offers new insights into these interactions with results that are both surprising and satisfying in the context of Rho's emerging structure. These include the requirements for binding and ATPase activation by a variety of RNA substrates, dynamic analyses of Rho tracking, heiicase and termination activity, and the participation of a new factor (NusG) that interacts with Rho. Models for Rho function are considered in the light of these recent revelations.

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Structural and functional properties of the segments of λ cro mRNA that interact with transcription termination factor Rho

Cited by 42 publications

References 28 publications

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

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

The nut site of bacteriophage lambda is made of RNA and is bound by transcription antitermination factors on the surface of RNA polymerase.

Rho and RNA: models for recognition and response

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