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Article

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

Journal of molecular biology - 19 Apr 1996

Martinez A, Opperman T, Richardson J P

Abstract excerpt

The function of transcription termination factor Rho from Escherichia coli is dependent upon its ability to bind to specific sites on nascent RNA molecules. The roles of 19 individual amino acid residues (Ile49 to Ser67) in and near a phylogenetically conserved sequence segment of Rho that is similar to the RNP1 motif found in many RNA-binding proteins were examined by testing the phenotypic consequences of...

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Identifiers

PMID: 8632473
DOI: 10.1006/jmbi.1996.0210

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mutational analysis and secondary structure model of the RNP1-like sequence motif of transcription termination factor Rho.PMID 8632473Read ↗

Residues in the RNP1-like sequence motif of Rho protein are involved in RNA-binding affinity and discrimination.Semantic proximity Read ↗

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

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

Mutational changes of conserved residues in the Q-loop region of transcription factor Rho greatly reduce secondary site RNA-binding.Semantic proximity Read ↗

Sequence-specific Rho-RNA interactions in transcription termination.Semantic proximity Read ↗

In vitro characterization of transcription termination factor Rho from Escherichia coli rho(nusD) mutants.Semantic proximity Read ↗

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

The bicyclomycin sensitivities of 38 bicyclomycin-resistant mutants of transcription termination protein rho and the location of their mutations support a structural model of rho based on the F(1) ATPase.Semantic proximity Read ↗

Mutations in the ATP-binding domain of Escherichia coli rho factor affect transcription termination in vivo.Semantic proximity Read ↗

Phenotypic characterization of a comprehensive set of bicyclomycin-resistant mutants.Semantic proximity Read ↗

Localization of nusA-suppressing amino acid substitutions in the conserved regions of the beta' subunit of Escherichia coli RNA polymerase.Semantic proximity Read ↗

Sequence-specific interactions in the RNA-binding domain of Escherichia coli transcription termination factor Rho.Semantic proximity Read ↗

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