Mutations in an RNP1 consensus sequence of Rho protein reduce RNA binding affinity but facilitate helicase turnover.

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Article

Mutations in an RNP1 consensus sequence of Rho protein reduce RNA binding affinity but facilitate helicase turnover.

The Journal of biological chemistry - 15 Sept 1991

Brennan C A, Platt T

Abstract excerpt

Escherichia coli rho protein facilitates transcription termination by a mechanism that involves rho binding to the nascent RNA, activation of rho's RNA-dependent ATPase activity, and release of the mRNA from the DNA template. The initial step, formation of a rho-RNA complex, is mediated primarily by an RNA binding domain included within the amino-terminal 151 amino acids of rho protein. We have now identified one...

Topics

Adenosine Triphosphatases
Adenosine Triphosphate
Alanine
Amino Acid Sequence
Base Sequence
Carrier Proteins
Consensus Sequence
DNA, Bacterial
Escherichia coli
Kinetics
Leucine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Molecular Sequence Data

Mutagenesis, Site-Directed

Mutation

Phenylalanine

RNA, Bacterial

RNA-Binding Proteins

Rho Factor

Source

Open in PubMed

Identifiers

PMID: 1716628

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1716628-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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Mutations in an RNP1 consensus sequence of Rho protein reduce RNA binding affinity but facilitate helicase turnover.PMID 1716628Read ↗

Mutational analysis and secondary structure model of the RNP1-like sequence motif of transcription termination factor Rho.Semantic proximity Read ↗

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Transcription termination defective mutants of Rho: role of different functions of Rho in releasing RNA from the elongation complex.Semantic proximity Read ↗

Analysis of E. coli rho factor: mutations affecting secondary-site interactions.Semantic proximity Read ↗

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