Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Functional complementation between mutations at two distant positions in Escherichia coli RNA polymerase as revealed by second-site suppression.

Molecular & general genetics : MGG - 1 Jan 2001

Sujatha S, Ishihama A, Chatterji D

Abstract excerpt

Subunit-subunit interactions are critical for the assembly of the core of Escherichia coli RNA polymerase. The mutant alpha-subunit C131A is unable to complement the temperature-sensitive alpha-R45C mutant strain, which is defective for binding of the beta-subunit. In vitro reconstitution experiments, however, indicate that the alpha-C131A variant is able to form the intermediate alpha2beta, but is defective in...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Aspartic Acid
Share to Chromatography, Gel

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Crystallography, X-Ray

Share to DNA-Directed RNA Polymerases

Share to Glycine

Share to Protein Structure, Secondary

Share to Suppression, Genetic

Share to Temperature

Source

Identifiers

PMID: 11212907
DOI: 10.1007/s004380000353

Provenance

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

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Functional complementation between mutations at two distant positions in Escherichia coli RNA polymerase as revealed by second-site suppression.PMID 11212907Read ↗

Identifying interacting regions in the beta subunit of Escherichia coli RNA polymerase.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 ↗

Functional map of the alpha subunit of Escherichia coli RNA polymerase: insertion analysis of the amino-terminal assembly domain.Semantic proximity Read ↗

Exploring the Amino Acid Residue Requirements of the RNA Polymerase (RNAP) α Subunit C-Terminal Domain for Productive Interaction between Spx and RNAP of Bacillus subtilis.Semantic proximity Read ↗

The effect of a nested set of C-terminal substituted deletions on the function of the alpha subunit of Escherichia coli RNA polymerase.Semantic proximity Read ↗

Pleiotropic effects of the rpoC10 mutation affecting the RNA polymerase beta' subunit of Escherichia coli on factor-dependent transcription termination and antitermination.Semantic proximity Read ↗

A functional relationship between helix 1 and the 900 tetraloop of 16S ribosomal RNA within the bacterial ribosome.Semantic proximity Read ↗

Loss of the Rpb4/Rpb7 subcomplex in a mutant form of the Rpb6 subunit shared by RNA polymerases I, II, and III.Semantic proximity Read ↗

Mutations in β' subunit of Escherichia coli RNA polymerase perturb the activator polymerase functional interaction required for promoter clearance.Semantic proximity Read ↗

Amber mutations in ribosome recycling factors of Escherichia coli and Thermus thermophilus: evidence for C-terminal modulator element.Semantic proximity Read ↗

A temperature-sensitive mutant of Escherichia coli affected in the alpha subunit of RNA polymerase.Semantic proximity Read ↗

Temperature-sensitive suppressor mutations of the Escherichia coli DNA gyrase B protein.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.