Evidence map›Paper›PMID 26283368›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2015

Regulated proteolysis of a cross-link-specific peptidoglycan hydrolase contributes to bacterial morphogenesis.

Santosh Kumar Singh, Sadiya Parveen, L SaiSree, Manjula Reddy

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 86 papers.

0numbers the graph read from it
0cells of the map it votes in
86citing papers in PubMed
4.9field-weighted citation impact, top 5% 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

86 citing papers in PubMed, 140 citations in OpenAlex.

  1. Review
  2. Article
  3. Peptidoglycan remodeling improves salt resilience ofApplied and environmental microbiology · 2026
    Article
  4. Review
  5. A conserved hub protein required for peptidoglycan remodeling and cell division inProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Article
  7. Control of theJournal of bacteriology · 2025
    Article
  8. Article
  9. Article
  10. Article
  11. A periplasmic protein modulates the proteolysis of peptidoglycan hydrolases to maintain cell wall homeostasis inProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  12. Article
  13. Article
  14. Journal of bacteriology · 2024
    Article
  15. The intrinsic macrolide resistome ofAntimicrobial agents and chemotherapy · 2024
    Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Article

26 more citing papers are in PubMed but not listed here.

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.

Santosh Kumar SinghCentre for Cellular and Molecular Biology, Hyderabad, India 500007.
Sadiya ParveenCentre for Cellular and Molecular Biology, Hyderabad, India 500007.
L SaiSreeCentre for Cellular and Molecular Biology, Hyderabad, India 500007.
Manjula ReddyCentre for Cellular and Molecular Biology, Hyderabad, India 500007 manjula@ccmb.res.in.
Centre for Cellular and Molecular Biology · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bacterial growth and morphogenesis are intimately coupled to expansion of peptidoglycan (PG), an extensively cross-linked macromolecule that forms a protective mesh-like sacculus around the cytoplasmic membrane. Growth of the PG sacculus is a dynamic event requiring the concerted action of hydrolases that cleave the cross-links for insertion of new material and synthases that catalyze cross-link formation; however, the factors that regulate PG expansion during bacterial growth are poorly understood. Here, we show that the PG hydrolase MepS (formerly Spr), which is specific to cleavage of cross-links during PG expansion in Escherichia coli, is modulated by proteolysis. Using combined genetic, molecular, and biochemical approaches, we demonstrate that MepS is rapidly degraded by a proteolytic system comprising an outer membrane lipoprotein of unknown function, NlpI, and a periplasmic protease, Prc (or Tsp). In summary, our results indicate that the NlpI-Prc system contributes to growth and enlargement of the PG sacculus by modulating the cellular levels of the cross-link-cleaving hydrolase MepS. Overall, this study signifies the importance of PG cross-link cleavage and its regulation in bacterial cell wall biogenesis.

Indexed as

MorphogenesisCross-Linking ReagentsEscherichia coliEscherichia coli ProteinsN-Acetylmuramoyl-L-alanine AmidasePeptidoglycanProteolysisCross-Linking ReagentsEscherichia coli ProteinsN-Acetylmuramoyl-L-alanine AmidasePeptidoglycanbacterial morphogenesisMepSNlpI-Prcpeptidoglycanregulated proteolysis

Identifiers

PMID26283368
PMCPMC4568209
OpenAlexW1962239550

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.