Evidence map›Paper›PMID 21746899›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

tRNA-dependent peptide bond formation by the transferase PacB in biosynthesis of the pacidamycin group of pentapeptidyl nucleoside antibiotics.

Wenjun Zhang, Ioanna Ntai, Neil L Kelleher, Christopher T Walsh

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
6.2field-weighted citation impact, top 4% 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

32 citing papers in PubMed, 64 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. A [3Fe-4S] cluster and tRNA-dependent aminoacyltransferase BlsK in the biosynthesis of Blasticidin S.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  6. Review
  7. Small-Molecule Acetylation by GCN5-RelatedMicrobiology and molecular biology reviews : MMBR · 2020
    Review
  8. Nonribosomal Peptide Extension by a Peptide Amino-Acyl tRNA Ligase.Journal of the American Chemical Society · 2019
    Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Review
  16. Article
  17. Article
  18. Review
  19. Natural and engineered biosynthesis of nucleoside antibiotics in Actinomycetes.Journal of industrial microbiology & biotechnology · 2016
    Review
  20. Review
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 3 institutions in 1 country.

Wenjun ZhangDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.
Ioanna Ntai
Neil L Kelleher
Christopher T Walsh
Northwestern University · USHarvard University · USUniversity of California, Berkeley · US

Funding

The Vancomycin Biosynthetic Assembly lineR01GM049338 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI WALSH, CHRISTOPHER T · 1993 to 2012
$6.2M
Mass Spectrometric Studies of Thiotemplate BiosynthesisR01GM067725 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI KELLEHER, NEIL L · 2003 to 2013
$3.0M
NIGMS NIH HHS GM067725-08NIGMS NIH HHS GM49338NIGMS NIH HHS R01 GM049338NIGMS NIH HHS R01 GM067725
6 · The paper itself

Abstract

Pacidamycins are a family of uridyl tetra/pentapeptide antibiotics with antipseudomonal activities through inhibition of the translocase MraY in bacterial cell wall assembly. The biosynthetic gene cluster for pacidamycins has recently been identified through genome mining of the producer Streptomyces coeruleorubidus, and the highly dissociated nonribosomal peptide assembly line for the uridyl tetrapeptide scaffold of pacidamycin has been characterized. In this work a hypothetical protein PacB, conserved in known uridyl peptide antibiotics gene clusters, has been characterized by both genetic deletion and enzymatic analysis of the purified protein. PacB catalyzes the transfer of the alanyl residue from alanyl-tRNA to the N terminus of the tetrapeptide intermediate yielding a pentapeptide on the thio-templated nonribosomal peptide synthetase (NRPS) assembly line protein PacH. PacB thus represents a new group of tRNA-dependent peptide bond-forming enzymes in secondary metabolite biosynthesis in addition to the recently identified cyclodipeptide synthases. The characterization of PacB completes the assembly line reconstitution of pacidamycin pentapeptide antibiotic scaffolds, bridging the primary and secondary metabolic pathways by hijacking an aminoacyl-tRNA to the antibiotic biosynthetic pathway.

Indexed as

Peptide BiosynthesisAmino Acid SequenceAminoacyltransferasesAnti-Bacterial AgentsBacterial ProteinsBase SequenceComputational BiologyDNA, BacterialGenes, BacterialModels, MolecularMolecular Sequence DataMultigene FamilyPeptidesPeptidyl TransferasesPyrimidine NucleosidesRecombinant ProteinsAminoacyltransferasesAnti-Bacterial AgentsBacterial ProteinsDNA, BacterialPeptidesPeptidyl TransferasesPyrimidine NucleosidesRecombinant ProteinsRNA, Transfer, Amino Acyl

Identifiers

PMID21746899
PMCPMC3145694
OpenAlexW2029264006

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.