Evidence map›Paper›PMID 25697505›Full record

ArticleNucleic acids research2015

CarD stabilizes mycobacterial open complexes via a two-tiered kinetic mechanism.

Jayan Rammohan, Ana Ruiz Manzano, Ashley L Garner, Christina L Stallings, Eric A Galburt

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

52 citing papers in PubMed, 75 citations in OpenAlex.

  1. Journal of bacteriology · 2026
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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

5 authors at 1 institution in 1 country.

Jayan RammohanDepartment of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO 63110, USA.
Ana Ruiz ManzanoDepartment of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO 63110, USA.
Ashley L GarnerDepartment of Molecular Microbiology, Washington University School of Medicine, St. Louis, MO 63110, USA.
Christina L StallingsDepartment of Molecular Microbiology, Washington University School of Medicine, St. Louis, MO 63110, USA.
Eric A GalburtDepartment of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO 63110, USA egalburt@biochem.wustl.edu.
Washington University in St. Louis · US

Funding

TRAINING PROGRAM IN CELLULAR AND MOLECULAR BIOLOGYT32GM007067 · NIGMS · WASHINGTON UNIVERSITY · PI TRUE-KROB, HEATHER L · 1985 to 2020
$20.4M
INVESTIGATING NOVEL MECHANISMS OF TRANSCRIPTION INITIATION REGULATION IN MYCOBACTERIAR01GM107544 · NIGMS · WASHINGTON UNIVERSITY · PI GALBURT, ERIC A, STALLINGS, CHRISTINA LEIGH · 2013 to 2017
$1.5M
NIGMS NIH HHS GM007067NIGMS NIH HHS R01 GM107544NIGMS NIH HHS R01GM107544
6 · The paper itself

Abstract

CarD is an essential and global transcriptional regulator in mycobacteria. While its biological role is unclear, CarD functions by interacting directly with RNA polymerase (RNAP) holoenzyme promoter complexes. Here, using a fluorescent reporter of open complex, we quantitate RPo formation in real time and show that Mycobacterium tuberculosis CarD has a dramatic effect on the energetics of RNAP bound complexes on the M. tuberculosis rrnAP3 ribosomal RNA promoter. The data reveal that Mycobacterium bovis RNAP exhibits an unstable RPo that is stabilized by CarD and suggest that CarD uses a two-tiered, concentration-dependent mechanism by associating with open and closed complexes with different affinities. Specifically, the kinetics of open-complex formation can be explained by a model where, at saturating concentrations of CarD, the rate of bubble collapse is slowed and the rate of opening is accelerated. The kinetics and open-complex stabilities of CarD mutants further clarify the roles played by the key residues W85, K90 and R25 previously shown to affect CarD-dependent gene regulation in vivo. In contrast to M. bovis RNAP, Escherichia coli RNAP efficiently forms RPo on rrnAP3, suggesting an important difference between the polymerases themselves and highlighting how transcriptional machinery can vary across bacterial genera.

Indexed as

Amino Acid SubstitutionBacterial ProteinsDNA, BacterialDNA-Directed RNA PolymerasesEscherichia coliEscherichia coli ProteinsKineticsModels, BiologicalMutagenesis, Site-DirectedMycobacteriumMycobacterium bovisMycobacterium tuberculosisPromoter Regions, GeneticRNA, BacterialRNA, RibosomalThermodynamicsBacterial ProteinsDNA, BacterialDNA-Directed RNA PolymerasesEscherichia coli ProteinsRNA, BacterialRNA, RibosomalTranscription Factors

Identifiers

PMID25697505
PMCPMC4381055
OpenAlexW2074293686

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.