Evidence map›Paper›PMID 20194510›Full record

ArticleThe Journal of biological chemistry2010

Evolution and multifarious horizontal transfer of an alternative biosynthetic pathway for the alternative polyamine sym-homospermidine.

Frances L Shaw, Katherine A Elliott, Lisa N Kinch, Christine Fuell, Margaret A Phillips, Anthony J Michael

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
1.4field-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

29 citing papers in PubMed, 62 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. The cell biology and genome ofMolecular biology of the cell · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Functional polyamine metabolic enzymes and pathways encoded by the virosphere.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  11. Article
  12. Article
  13. Article
  14. The tree of life of polyamine oxidases.Scientific reports · 2020
    Article
  15. Article
  16. Article
  17. Article
  18. Polyamines in Eukaryotes, Bacteria, and Archaea.The Journal of biological chemistry · 2016
    Review
  19. Article
  20. 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

6 authors at 3 institutions in 2 countries.

Frances L ShawInstitute of Food Research, Norwich Research Park, Colney, Norwich NR4 7UA, United Kingdom.
Katherine A Elliott
Lisa N Kinch
Christine Fuell
Margaret A Phillips
Anthony J Michael
Norwich Research Park · GBQuadram Institute · GBThe University of Texas Southwestern Medical Center · US

Funding

TRYPANSOMIASIS--MOLECULAR APPROACHES TO CHEMOTHERAPYR01AI034432 · NIAID · UT SOUTHWESTERN MEDICAL CENTER · PI PHILLIPS, MARGARET A. · 1995 to 2024
$4.9M
Polyamine and trypanothione metabolism in Trypanosoma bruceiR37AI034432 · NIAID · UT SOUTHWESTERN MEDICAL CENTER · PI PHILLIPS, MARGARET A. · 2009 to 2018
$4.0M
Biotechnology and Biological Sciences Research CouncilNIAID NIH HHS R01 AI034432NIAID NIH HHS R01 AI34432NIAID NIH HHS R37 AI034432
6 · The paper itself

Abstract

Polyamines are small flexible organic polycations found in almost all cells. They likely existed in the last universal common ancestor of all extant life, and yet relatively little is understood about their biological function, especially in bacteria and archaea. Unlike eukaryotes, where the predominant polyamine is spermidine, bacteria may contain instead an alternative polyamine, sym-homospermidine. We demonstrate that homospermidine synthase (HSS) has evolved vertically, primarily in the alpha-Proteobacteria, but enzymatically active, diverse HSS orthologues have spread by horizontal gene transfer to other bacteria, bacteriophage, archaea, eukaryotes, and viruses. By expressing diverse HSS orthologues in Escherichia coli, we demonstrate in vivo the production of co-products diaminopropane and N(1)-aminobutylcadaverine, in addition to sym-homospermidine. We show that sym-homospermidine is required for normal growth of the alpha-proteobacterium Rhizobium leguminosarum. However, sym-homospermidine can be replaced, for growth restoration, by the structural analogues spermidine and sym-norspermidine, suggesting that the symmetrical or unsymmetrical form and carbon backbone length are not critical for polyamine function in growth. We found that the HSS enzyme evolved from the alternative spermidine biosynthetic pathway enzyme carboxyspermidine dehydrogenase. The structure of HSS is related to lysine metabolic enzymes, and HSS and carboxyspermidine dehydrogenase evolved from the aspartate family of pathways. Finally, we show that other bacterial phyla such as Cyanobacteria and some alpha-Proteobacteria synthesize sym-homospermidine by an HSS-independent pathway, very probably based on deoxyhypusine synthase orthologues, similar to the alternative homospermidine synthase found in some plants. Thus, bacteria can contain alternative biosynthetic pathways for both spermidine and sym-norspermidine and distinct alternative pathways for sym-homospermidine.

Indexed as

Biological EvolutionBiosynthetic PathwaysAlkyl and Aryl TransferasesBacteriaChromatography, High Pressure LiquidModels, MolecularPhylogenyPolyaminesSpermidineAlkyl and Aryl Transferaseshomospermidine synthetasePolyaminesSpermidinesym-homospermidine

Identifiers

PMID20194510
PMCPMC2863184
OpenAlexW2091510265

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.