Evidence map›Paper›PMID 28842486›Full record

ArticleThe Journal of biological chemistry2017

The bacterial condensin MukB compacts DNA by sequestering supercoils and stabilizing topologically isolated loops.

Rupesh Kumar, Małgorzata Grosbart, Pearl Nurse, Soon Bahng, Claire L Wyman, Kenneth J Marians

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
–field-weighted citation impact
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

19 citing papers in PubMed.

  1. Analysis of Human miRNA Derived From Bladder Epithelial Cells Infected With Uropathogenic Escherichia coli.APMIS : acta pathologica, microbiologica, et immunologica Scandinavica · 2026
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  2. Review
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  16. Dissecting DNA Compaction by the Bacterial Condensin MukB.Methods in molecular biology (Clifton, N.J.) · 2019
    Article
  17. Small Molecule Condensin Inhibitors.ACS infectious diseases · 2018
    Article
  18. Article
  19. Article
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.

Rupesh KumarFrom the Molecular Biology Program, Memorial Sloan Kettering Cancer Center, New York, New York 10065 and.
Małgorzata Grosbartthe Departments of Molecular Genetics and.
Pearl NurseFrom the Molecular Biology Program, Memorial Sloan Kettering Cancer Center, New York, New York 10065 and.
Soon BahngFrom the Molecular Biology Program, Memorial Sloan Kettering Cancer Center, New York, New York 10065 and.
Claire L Wymanthe Departments of Molecular Genetics and.
Kenneth J MariansFrom the Molecular Biology Program, Memorial Sloan Kettering Cancer Center, New York, New York 10065 and kmarians@sloankettering.edu.

Funding

X-RAY CRYSTALLOGRAPHYP30CA008748 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI Nicholas D Socci · 1985 to 2026
$347.4M
Topoisomerases, Condensins, and Chromosome SegregationR01GM034558 · NIGMS · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI MARIANS, KENNETH J · 1985 to 2017
$6.6M
NCI NIH HHS P30 CA008748NIGMS NIH HHS R01 GM034558
6 · The paper itself

Abstract

MukB is a structural maintenance of chromosome-like protein required for DNA condensation. The complete condensin is a large tripartite complex of MukB, the kleisin, MukF, and an accessory protein, MukE. As found previously, MukB DNA condensation is a stepwise process. We have defined these steps topologically. They proceed first via the formation of negative supercoils that are sequestered by the protein followed by hinge-hinge interactions between MukB dimers that stabilize topologically isolated loops in the DNA. MukB itself is sufficient to mediate both of these topological alterations; neither ATP nor MukEF is required. We show that the MukB hinge region binds DNA and that this region of the protein is involved in sequestration of supercoils. Cells carrying mutations in the MukB hinge that reduce DNA condensation

Indexed as

Protein MultimerizationChromosomal Proteins, Non-HistoneDNA, BacterialDNA, SuperhelicalEscherichia coliEscherichia coli ProteinsMutationRepressor ProteinsChromosomal Proteins, Non-HistoneDNA, BacterialDNA, SuperhelicalEscherichia coli ProteinsMukB protein, E colimukE protein, E colimukF protein, E coliRepressor ProteinschromosomesDNADNA enzymesDNA structureDNA topologynucleic acid enzymesnucleic acid enzymologynucleic acids

Identifiers

PMID28842486
PMCPMC5641887

What OpenQuestion holds

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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.