Evidence map›Paper›PMID 26299947›Full record

ArticleStructure (London, England : 1993)2015

Structure of Ribosomal Silencing Factor Bound to Mycobacterium tuberculosis Ribosome.

Xiaojun Li, Qingan Sun, Cai Jiang, Kailu Yang, Li-Wei Hung, Junjie Zhang, James C Sacchettini

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

29 citing papers in PubMed, 59 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Mechanistic insights intobioRxiv : the preprint server for biology · 2026
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Y98 Mutation Leads to the Loss of RsfS Anti-Association Activity inInternational journal of molecular sciences · 2022
    Article
  10. Review
  11. HflX is a GTPase that controls hypoxia-induced replication arrest in slow-growing mycobacteria.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  12. Article
  13. Article
  14. Structure of the mature kinetoplastids mitoribosome and insights into its large subunit biogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 1 country.

Xiaojun LiDepartment of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843, USA.
Qingan SunDepartment of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843, USA.
Cai JiangDepartment of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843, USA.
Kailu YangDepartment of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843, USA.
Li-Wei HungLawrence Berkeley National Laboratory, University of California, Berkeley, CA 94720, USA.
Junjie ZhangDepartment of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843, USA. Electronic address: junjiez@tamu.edu.
James C SacchettiniDepartment of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843, USA. Electronic address: sacchett@tamu.edu.
Texas A&M University · USUniversity of California, Berkeley · US

Funding

Vulnerabilities in Mycobacterial Cell-Wall BiogenesisP01AI095208 · NIAID · UNIVERSITY OF CALIFORNIA-IRVINE · PI ZHANG, JUNJIE · 2012 to 2022
$19.8M
Howard Hughes Medical InstituteNIAID NIH HHS P01 AI095208NIAID NIH HHS P01AI095208
6 · The paper itself

Abstract

The ribosomal silencing factor RsfS slows cell growth by inhibiting protein synthesis during periods of diminished nutrient availability. The crystal structure of Mycobacterium tuberculosis (Mtb) RsfS, together with the cryo-electron microscopy (EM) structure of the large subunit 50S of Mtb ribosome, reveals how inhibition of protein synthesis by RsfS occurs. RsfS binds to the 50S at L14, which, when occupied, blocks the association of the small subunit 30S. Although Mtb RsfS is a dimer in solution, only a single subunit binds to 50S. The overlap between the dimer interface and the L14 binding interface confirms that the RsfS dimer must first dissociate to a monomer in order to bind to L14. RsfS interacts primarily through electrostatic and hydrogen bonding to L14. The EM structure shows extended rRNA density that it is not found in the Escherichia coli ribosome, the most striking of these being the extended RNA helix of H54a.

Indexed as

Gene Expression Regulation, BacterialProtein BiosynthesisBacterial ProteinsBinding SitesCryoelectron MicroscopyCrystallography, X-RayEscherichia coliModels, MolecularMycobacterium smegmatisMycobacterium tuberculosisProtein BindingProtein MultimerizationProtein Structure, SecondaryProtein Structure, TertiaryRecombinant ProteinsRibosomal ProteinsBacterial ProteinsRecombinant ProteinsRibosomal ProteinsRNA, BacterialRNA, RibosomalTranscription Factors

Identifiers

PMID26299947
PMCPMC4718548
OpenAlexW1882341309

What OpenQuestion holds

Textmetadata
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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.