Evidence map›Paper›PMID 26031910›Full record

ArticleJournal of bacteriology2015

Genetic and Proteomic Analyses of Pupylation in Streptomyces coelicolor.

Corey L Compton, Michael S Fernandopulle, Rohith T Nagari, Jason K Sello

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

22 citing papers in PubMed, 36 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Streptomyces coelicolor Vesicles: Many Molecules To Be Delivered.Applied and environmental microbiology · 2022
    Article
  8. Review
  9. Review
  10. Review
  11. Review
  12. Protein post-translational modifications in bacteria.Nature reviews. Microbiology · 2019
    Review
  13. Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Bacterial Proteasomes: Mechanistic and Functional Insights.Microbiology and molecular biology reviews : MMBR · 2017
    Review
  19. Article
  20. The pupylation machinery is involved in iron homeostasis by targeting the iron storage protein ferritin.Proceedings of the National Academy of Sciences of the United States of America · 2016
    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

4 authors at 1 institution in 1 country.

Corey L ComptonDepartment of Chemistry, Brown University, Providence, Rhode Island, USA.
Michael S FernandopulleDepartment of Chemistry, Brown University, Providence, Rhode Island, USA.
Rohith T NagariDepartment of Chemistry, Brown University, Providence, Rhode Island, USA.
Jason K SelloDepartment of Chemistry, Brown University, Providence, Rhode Island, USA jason_sello@brown.edu.
Brown University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

unlabelledPupylation is a posttranslational modification peculiar to actinobacteria wherein proteins are covalently modified with a small protein called the prokaryotic ubiquitin-like protein (Pup). Like ubiquitination in eukaryotes, this phenomenon has been associated with proteasome-mediated protein degradation in mycobacteria. Here, we report studies of pupylation in a streptomycete that is phylogentically related to mycobacteria. We constructed mutants of Streptomyces coelicolor lacking PafA (Pup ligase), the proteasome, and the Pup-proteasome system. We found that these mutants share a high susceptibility to oxidative stress compared to that of the wild-type strain. Remarkably, we found that the pafA null mutant has a sporulation defect not seen in strains lacking the Pup-proteasome system. In proteomics experiments facilitated by an affinity-tagged variant of Pup, we identified 110 pupylated proteins in S. coelicolor strains having and lacking genes encoding the 20S proteasome. Our findings shed new light on this unusual posttranslational modification and its role in Streptomyces physiology. IMPORTANCE: The presence of 20S proteasomes reminiscent of those in eukaryotes and a functional equivalent of ubiquitin, known as the prokaryotic ubiquitin-like protein (Pup), in actinobacteria have motivated reevaluations of protein homeostasis in prokaryotes. Though the Pup-proteasome system has been studied extensively in mycobacteria, it is much less understood in streptomycetes, members of a large genus of actinobacteria known for highly choreographed life cycles in which phases of morphological differentiation, sporulation, and secondary metabolism are often regulated by protein metabolism. Here, we define constituents of the pupylome in Streptomyces coelicolor for the first time and present new evidence that links pupylation and the oxidative stress response in this bacterium. Surprisingly, we found that the Pup ligase has a Pup-independent role in sporulation.

Indexed as

Amino Acid SequenceAnimalsBacterial ProteinsGene Expression Regulation, BacterialMolecular Sequence DataMutationProtein Processing, Post-TranslationalProteomicsPupaStreptomyces coelicolorUbiquitinsBacterial ProteinsUbiquitins

Identifiers

PMID26031910
PMCPMC4524032
OpenAlexW1621832841

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.