SGD Paper 
Kashiwagi K and Igarashi K (2011) Identification and Assays of Polyamine Transport Systems in Escherichia coli and Saccharomyces cerevisiae. Methods Mol Biol 720():295-308
Abstract: Polyamine content in cells is regulated by biosynthesis, degradation, and transport. With regard to transport, uptake and excretion proteins exist in Escherichia coli and Saccharomyces cerevisiae. In E. coli, the uptake systems comprise a spermidine-preferential uptake system consisting of the PotA, B, C, and D proteins, and a putrescine-specific uptake system consisting of the PotF, G, H, and I proteins. Two other proteins, PotE and CadB, each containing 12 transmembrane segments, function as antiporters (putrescine-ornithine and cadaverine-lysine) and are important for cell growth at acidic pH. MdtJI was identified as a spermidine excretion system. When putrescine was used as energy source, PuuP functioned as a putrescine transporter. In S. cerevisiae, DUR3 and SAM3, containing 16 or 12 transmembrane segments, are the major polyamine uptake proteins, whereas TPO1 and TPO5, containing 12 transmembrane segments, are the major polyamine excretion proteins, and UGA4 is a putrescine transporter on the vacuolar membrane. The activities of DUR3 and TPO1 are regulated by phosphorylation of serine/threonine residues. The identification and assay procedures of these transporters are described in this chapter.
| Status: Published | Type: Journal Article | PubMed ID: 21318881 |
Topics addressed in this paper
Number of different genes curated to this paper: 5
- To find other papers on a gene and topic, click on the colored ball in the appropriate box.
- displays other papers with information about that topic for that gene.
- displays other papers in SGD that are associated with that topic.
The topic is addressed in these papers but does not describe a specific gene or chromosomal feature.
- To go to the Locus page for a gene, click on the gene name.
