Evidence map›Paper›PMID 23771146›Full record

ArticleNucleic acids research2013

Cooperativity and interaction energy threshold effects in recognition of the -10 promoter element by bacterial RNA polymerase.

Vladimir Mekler, Konstantin Severinov

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2013. 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
2.1field-weighted citation impact, top 13% 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, 13 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

2 authors at 1 institution in 2 countries.

Vladimir MeklerDepartment of Molecular Biology and Biochemistry, Waksman Institute of Microbiology Rutgers, State University of New Jersey, Piscataway, NJ 08854, USA and Institutes of Molecular Genetics and Gene Biology, Russian Academy of Sciences, Moscow 119334, Russia.
Konstantin Severinov
Rutgers, The State University of New Jersey · US

Funding

Phage-induced modifications of RNA polymeraseR01GM059295 · NIGMS · RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK · PI SEVERINOV, KONSTANTIN V · 1999 to 2013
$4.5M
Structure-based mutational analysis of RNA polymeraseR01GM064530 · NIGMS · RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK · PI SEVERINOV, KONSTANTIN V · 2002 to 2010
$2.7M
NIGMS NIH HHS R01GM59295NIGMS NIH HHS R01 GM64530
6 · The paper itself

Abstract

RNA polymerase (RNAP) melts promoter DNA to form transcription-competent open promoter complex (RPo). Interaction of the RNAP σ subunit with non-template strand bases of a conserved -10 element (consensus sequence T-12A-11T-10A-9A-8T-7) is an important source of energy-driving localized promoter melting. Here, we used an RNAP molecular beacon assay to investigate interdependencies of RNAP interactions with -10 element nucleotides. The results reveal a strong cooperation between RNAP interactions with individual -10 element non-template strand nucleotides and indicate that recognition of the -10 element bases occurs only when free energy of the overall RNAP -10 element binding reaches a certain threshold level. The threshold-like mode of the -10 element recognition may be related to the energetic cost of attaining a conformation of the -10 element that is recognizable by RNAP. The RNAP interaction with T/A-12 base pair was found to be strongly stimulated by RNAP interactions with other -10 element bases and with promoter spacer between the -10 and -35 promoter elements. The data also indicate that unmelted -10 promoter element can impair RNAP interactions with promoter DNA upstream of the -11 position. We suggest that cooperativity and threshold effects are important factors guiding the dynamics and selectivity of RPo formation.

Indexed as

Promoter Regions, GeneticBacterial ProteinsBase PairingConsensus SequenceDNA, BacterialDNA-Directed RNA PolymerasesDNA, IntergenicEnergy TransferEscherichia coliHoloenzymesMultiprotein ComplexesNucleic Acid ConformationProtein BindingProtein Interaction MappingTranscription, GeneticBacterial ProteinsDNA, BacterialDNA-Directed RNA PolymerasesDNA, IntergenicHoloenzymesMultiprotein Complexes

Identifiers

PMID23771146
PMCPMC3753650
OpenAlexW2012589580

What OpenQuestion holds

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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.