Evidence map›Paper›PMID 34795302›Full record

ArticleNature communications2021

Acyl carrier protein promotes MukBEF action in Escherichia coli chromosome organization-segregation.

Josh P Prince, Jani R Bolla, Gemma L M Fisher, Jarno Mäkelä, Marjorie Fournier, Carol V Robinson, Lidia K Arciszewska, David J Sherratt

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

12 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. RSC chemical biology · 2026
    Article
  3. bioRxiv : the preprint server for biology · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Structural biology of SMC complexes across the tree of life.Current opinion in structural biology · 2023
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. 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

8 authors at 2 institutions in 2 countries.

Josh P PrinceDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK.ORCID http://orcid.org/0000-0003-0877-7538
Jani R BollaPhysical and Theoretical Chemistry Laboratory, University of Oxford, South Parks Road, Oxford, OX1 3QZ, UK.ORCID http://orcid.org/0000-0003-4346-182X
Gemma L M FisherDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK.ORCID http://orcid.org/0000-0001-8468-5032
Jarno MäkeläDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK.ORCID http://orcid.org/0000-0003-1844-2619
Marjorie FournierDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK.
Carol V RobinsonPhysical and Theoretical Chemistry Laboratory, University of Oxford, South Parks Road, Oxford, OX1 3QZ, UK.ORCID http://orcid.org/0000-0001-7829-5505
Lidia K ArciszewskaDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK.
David J SherrattDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK. david.sherratt@bioch.ox.ac.uk.ORCID http://orcid.org/0000-0002-2104-5430
University of Oxford · GBCardiovascular Institute of the South · US

Funding

Medical Research Council MR/N020413/1Medical Research Council MR/V028839/1Wellcome Trust 200782/Z/16/ZWellcome Trust (Wellcome) 200782/Z/16/Z
6 · The paper itself

Abstract

Structural Maintenance of Chromosomes (SMC) complexes act ubiquitously to compact DNA linearly, thereby facilitating chromosome organization-segregation. SMC proteins have a conserved architecture, with a dimerization hinge and an ATPase head domain separated by a long antiparallel intramolecular coiled-coil. Dimeric SMC proteins interact with essential accessory proteins, kleisins that bridge the two subunits of an SMC dimer, and HAWK/KITE proteins that interact with kleisins. The ATPase activity of the Escherichia coli SMC protein, MukB, which is essential for its in vivo function, requires its interaction with the dimeric kleisin, MukF that in turn interacts with the KITE protein, MukE. Here we demonstrate that, in addition, MukB interacts specifically with Acyl Carrier Protein (AcpP) that has essential functions in fatty acid synthesis. We characterize the AcpP interaction at the joint of the MukB coiled-coil and show that the interaction is necessary for MukB ATPase and for MukBEF function in vivo.

Indexed as

Chromosome SegregationAcyl Carrier ProteinAdenosine TriphosphatasesChromosomal Proteins, Non-HistoneChromosomes, BacterialEnzyme ActivationEscherichia coliEscherichia coli ProteinsMutationProtein BindingRepressor ProteinsAcyl Carrier ProteinAdenosine TriphosphatasesChromosomal Proteins, Non-HistoneEscherichia coli ProteinsMukB protein, E colimukE protein, E colimukF protein, E coliRepressor Proteins

Identifiers

PMID34795302
PMCPMC8602292
OpenAlexW3214337704

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.