Evidence map›Paper›PMID 25385626›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

DNA topology confers sequence specificity to nonspecific architectural proteins.

Juan Wei, Luke Czapla, Michael A Grosner, David Swigon, Wilma K Olson

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

26 citing papers in PubMed, 41 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

5 authors at 2 institutions in 1 country.

Juan WeiDepartment of Chemistry and Chemical Biology, BioMaPS Institute for Quantitative Biology, Rutgers, the State University of New Jersey, Piscataway, NJ 08854; and.
Luke CzaplaDepartment of Chemistry and Chemical Biology, BioMaPS Institute for Quantitative Biology, Rutgers, the State University of New Jersey, Piscataway, NJ 08854; and.
Michael A GrosnerDepartment of Chemistry and Chemical Biology, BioMaPS Institute for Quantitative Biology, Rutgers, the State University of New Jersey, Piscataway, NJ 08854; and.
David SwigonDepartment of Mathematics, University of Pittsburgh, Pittsburgh, PA 15260.
Wilma K OlsonDepartment of Chemistry and Chemical Biology, BioMaPS Institute for Quantitative Biology, Rutgers, the State University of New Jersey, Piscataway, NJ 08854; and wilma.olson@rutgers.edu.
Rutgers, The State University of New Jersey · USUniversity of Pittsburgh · US

Funding

THEORETICFAL ASPECTS OF DNA SUPERCOILINGR01GM034809 · NIGMS · RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK · PI OLSON, WILMA K · 1985 to 2019
$4.6M
Computer Cluster for Computational and Structural BiologyS10RR022375 · NCRR · RUTGERS, THE STATE UNIV OF N.J. · PI LEVY, RONALD · 2007 to 2007
$291k
NCRR NIH HHS RR022375NCRR NIH HHS S10 RR022375NIGMS NIH HHS GM34809NIGMS NIH HHS R01 GM034809
6 · The paper itself

Abstract

Topological constraints placed on short fragments of DNA change the disorder found in chain molecules randomly decorated by nonspecific, architectural proteins into tightly organized 3D structures. The bacterial heat-unstable (HU) protein builds up, counter to expectations, in greater quantities and at particular sites along simulated DNA minicircles and loops. Moreover, the placement of HU along loops with the "wild-type" spacing found in the Escherichia coli lactose (lac) and galactose (gal) operons precludes access to key recognition elements on DNA. The HU protein introduces a unique spatial pathway in the DNA upon closure. The many ways in which the protein induces nearly the same closed circular configuration point to the statistical advantage of its nonspecificity. The rotational settings imposed on DNA by the repressor proteins, by contrast, introduce sequential specificity in HU placement, with the nonspecific protein accumulating at particular loci on the constrained duplex. Thus, an architectural protein with no discernible DNA sequence-recognizing features becomes site-specific and potentially assumes a functional role upon loop formation. The locations of HU on the closed DNA reflect long-range mechanical correlations. The protein responds to DNA shape and deformability—the stiff, naturally straight double-helical structure—rather than to the unique features of the constituent base pairs. The structures of the simulated loops suggest that HU architecture, like nucleosomal architecture, which modulates the ability of regulatory proteins to recognize their binding sites in the context of chromatin, may influence repressor-operator interactions in the context of the bacterial nucleoid.

Indexed as

DNADNA-Binding ProteinsOperonDNADNA-Binding ProteinsDNA cyclizationlac operonMonte Carlo simulationnonspecific bindingprotein-mediated looping

Identifiers

PMID25385626
PMCPMC4250108
OpenAlexW1970432442

What OpenQuestion holds

Textmetadata
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.