Evidence map›Paper›PMID 19019158›Full record

ArticleMolecular microbiology2008

A single aromatic residue in transcriptional repressor protein KorA is critical for cooperativity with its co-regulator KorB.

Lewis E H Bingle, Karthik V Rajasekar, Sidra tul Muntaha, Vinod Nadella, Eva I Hyde, Christopher M Thomas

Open access · bronzeAbstract read
In one paragraph

Article in Molecular microbiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.1field-weighted citation impact, top 19% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

10 citing papers in PubMed, 16 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 1 country.

Lewis E H BingleSchool of Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, UK.
Karthik V Rajasekar
Sidra tul Muntaha
Vinod Nadella
Eva I Hyde
Christopher M Thomas
University of Birmingham · GBUniversity of Cambridge · GB

Funding

Wellcome TrustWellcome Trust 067526/Z
6 · The paper itself

Abstract

A central feature of broad host range IncP-1 plasmids is the set of regulatory circuits that tightly control plasmid core functions under steady-state conditions. Cooperativity between KorB and either KorA or TrbA repressor proteins is a key element of these circuits and deletion analysis has implicated the conserved C-terminal domain of KorA and TrbA in this interaction. By NMR we show that KorA and KorB interact directly and identify KorA amino acids that are affected on KorB binding. Studies on mutants showed that tyrosine 84 (or phenylalanine, in some alleles) is dispensable for repressor activity but critical for the specific interaction with KorB in both in vivo reporter gene assays and in vitro electrophoretic mobility shift and co-purification assays. This confirms that direct and specific protein-protein interactions are responsible for the cooperativity observed between KorB and its corepressors and lays the basis for determining the biological importance of this cooperativity.

Indexed as

Amino Acid SequenceAmino Acid SubstitutionBacterial ProteinsDNAGene Expression Regulation, BacterialMolecular Sequence DataNuclear Magnetic Resonance, BiomolecularPhenylalaninePlasmidsProtein BindingProtein Interaction MappingProtein Structure, TertiaryRepressor ProteinsTranscription, GeneticTyrosineBacterial ProteinsDNAKorA protein, bacteriaKorB protein, Plasmid RK2PhenylalanineRepressor ProteinsTyrosine

Identifiers

PMID19019158
PMCPMC2680271
OpenAlexW2132333820

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.