ReviewThe Biochemical journal1999
Polyamine transport in bacteria and yeast.
Review in The Biochemical journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 91 papers.
What it found
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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.
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Who cites it
91 citing papers in PubMed, 257 citations in OpenAlex.
- Amino acid metabolism by pig intestinal bacteria and consequences for intestinal health and environment: current knowledge and future directions.Journal of animal science and biotechnology · 2026Review
- Recycling of Undigested Proteins Provided by the Host to the Large Intestine Microbiota: Implication for Intestinal Bacterial Anabolism, Growth, and Physiology.Microorganisms · 2025Review
- Quorum Sensing inMicroorganisms · 2025Article
- Structural insights into polyamine spermidine uptake by the ABC transporter PotD-PotABC.Science advances · 2024Article
- Salmonella Typhimurium exploits host polyamines for assembly of the type 3 secretion machinery.PLoS biology · 2024Article
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- Cationic Polymers Enable Internalization of Negatively Charged Chemical Probes into Bacteria.ACS chemical biology · 2023Article
- Elucidating the Role ofMedical sciences (Basel, Switzerland) · 2022Article
- Polyamine and Ethanolamine Metabolism in Bacteria as an Important Component of Nitrogen Assimilation for Survival and Pathogenicity.Medical sciences (Basel, Switzerland) · 2022Review
- Metagenomes of polyamine-transforming bacterioplankton along a nearshore-open ocean transect.Marine life science & technology · 2022Article
- Alternative Pathways to Ciprofloxacin Resistance in Neisseria gonorrhoeae: An In Vitro Study of the WHO-P and WHO-F Reference StrainsAntibiotics (Basel, Switzerland) · 2022Article
- Pathogenomes and variations in Shiga toxin production among geographically distinct clones ofMicrobial genomics · 2022Article
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- Investigation of the polyamine biosynthetic and transport capability ofMicrobiology (Reading, England) · 2021Article
- Structural basis of polyamine transport by human ATP13A2 (PARK9).Molecular cell · 2021Article
- SAR11 Cells Rely on Enzyme Multifunctionality To Metabolize a Range of Polyamine Compounds.mBio · 2021Article
- Phylogeny resolved, metabolism revealed: functional radiation within a widespread and divergent clade of sponge symbionts.The ISME journal · 2021Article
- Unlocking Cryptic Metabolites with Mass Spectrometry-Guided Transposon Mutant Selection.ACS chemical biology · 2020Article
- Article
- Characterization of ABC transporter genes, sll1180, sll1181, and slr1270, involved in acid stress tolerance of Synechocystis sp. PCC 6803.Photosynthesis research · 2019Article
31 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The polyamine content of cells is regulated by biosynthesis, degradation and transport. In Escherichia coli, the genes for three different polyamine transport systems have been cloned and characterized. Two uptake systems (putrescine-specific and spermidine-preferential) were ABC transporters, each consisting of a periplasmic substrate-binding protein, two transmembrane proteins and a membrane-associated ATPase. The crystal structures of the substrate-binding proteins (PotD and PotF) have been solved. They consist of two domains with an alternating beta-alpha-beta topology, similar to other periplasmic binding proteins. The polyamine-binding site is in a cleft between the two domains, as determined by crystallography and site-directed mutagenesis. Polyamines are mainly recognized by aspartic acid and glutamic acid residues, which interact with the NH(2)- (or NH-) groups, and by tryptophan and tyrosine residues that have hydrophobic interactions with the methylene groups of polyamines. The precursor of one of the substrate binding proteins, PotD, negatively regulates transcription of the operon for the spermidine-preferential uptake system, thus providing another level of regulation of cellular polyamines. The third transport system, catalysed by PotE, mediates both uptake and excretion of putrescine. Uptake of putrescine is dependent on membrane potential, whereas excretion involves an exchange reaction between putrescine and ornithine. In Saccharomyces cerevisiae, the gene for a polyamine transport protein (TPO1) was identified. The properties of this protein are similar to those of PotE, and TPO1 is located on the vacuolar membrane.
Indexed as
Identifiers
10585849PMC1220684W2023807790What OpenQuestion holds
Registered trials
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.