Characterization of ammonium transporters in the dinoflagellate Alexandrium catenella (Group I)

Clicks: 9
ID: 331559
2026
Article Quality & Performance Metrics
Overall Quality
Not rated
Combines reader engagement with the AI quality analysis. This article has not been analysed, so there is no overall score — reader engagement is measured and shown alongside.
AI Quality Assessment
Not analyzed
Readership in this journal
Emerging

Ranked #223 of 230 articles by views in FEMS microbiology letters

Most read Least read

Bar heights use a square-root scale. Only the 120 most-read articles are drawn; the journal has 230 in total.

Mint this article as an NFT
Not yet minted

Create a permanent, verifiable on-chain record of this article on the Scimatic Network. The NFT is held in your Journament account, and you can withdraw it to your own wallet at any time.

5 SUSD one-off · no wallet required
Abstract
Alexandrium catenella (Group I) causes paralytic shellfish poisoning. Nitrogen is a critical component for both growth and toxin production in A. catenella, and recent studies have indicated that A. catenella uses both inorganic nitrogen and ammonium as nitrogen sources. However, the molecular mechanism underlying the transportation of ammonium in A. catenella has not been identified. In this study, we attempted to isolate and characterize the ammonium transporter (AMT) in A. catenella. cDNA cloning produced a number of AMT clones. To investigate the ammonium transport capability of A. catenella AMT (AlcAMT), we selected three representative cDNAs​ and the clones were inserted into expression vectors. These vectors were then transferred into an amt-deficient Schizosaccharomyces pombe transgenic yeast strain and grown on a medium containing NH4Cl as the only nitrogen source. Following transformation, yeast transformants carrying only one of the three AMTs were able to grow on the medium, confirming its ability to transport ammonium. Sequence analysis of the three AMT variants revealed that the successful variant included a K residue at sequence position 450, while the other variants contained a T residue at the same position. Mutation analysis confirmed that K450 is important for the function of AlcAMT.
Reference Key
openalex_W7220681373 Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Atsushi Kobiyama, Shinkichi Okiyama, Yuichiro Yamada
Journal FEMS microbiology letters
Year 2026
DOI
10.1093/femsle/fnag120
URL
Keywords Keywords not found

Citations

No citations found. To add a citation, contact the admin at info@scimatic.org

No comments yet. Be the first to comment on this article.