A polyamine-independent role for S-adenosylmethionine decarboxylase

Bin Li, Shin Kurihara, Sok Ho Kim, Jue Liang, Anthony J Michael

Research output: Contribution to journalArticle

Abstract

The only known function of S-adenosylmethionine decarboxylase (AdoMetDC) is to supply, with its partner aminopropyltransferase enzymes such as spermidine synthase (SpdSyn), the aminopropyl donor for polyamine biosynthesis. Polyamine spermidine is probably essential for the growth of all eukaryotes, most archaea and many bacteria. Two classes of AdoMetDC exist, the prokaryotic class 1a and 1b forms, and the eukaryotic class 2 enzyme, which is derived from an ancient fusion of two prokaryotic class 1b genes. Herein, we show that 'eukaryotic' class 2 AdoMetDCs are found in bacteria and are enzymatically functional. However, the bacterial AdoMetDC class 2 genes are phylogenetically limited and were likely acquired from a eukaryotic source via transdomain horizontal gene transfer, consistent with the class 2 form of AdoMetDC being a eukaryotic invention. We found that some class 2 and thousands of class 1b AdoMetDC homologues are present in bacterial genomes that also encode a gene fusion of an N-terminal membrane protein of the Major Facilitator Superfamily (MFS) class of transporters and a C-terminal SpdSyn-like domain. Although these AdoMetDCs are enzymatically functional, spermidine is absent, and an entire fusion protein or its SpdSyn-like domain only, does not biochemically complement a SpdSyn deletion strain of E. coli This suggests that the fusion protein aminopropylates a substrate other than putrescine, and has a role outside of polyamine biosynthesis. Another integral membrane protein found clustered with these genes is DUF350, which is also found in other gene clusters containing a homologue of the glutathionylspermidine synthetase family and occasionally other polyamine biosynthetic enzymes.

Original languageEnglish (US)
Pages (from-to)2579-2594
Number of pages16
JournalThe Biochemical journal
Volume476
Issue number18
DOIs
StatePublished - Sep 20 2019

Fingerprint

Spermidine Synthase
Adenosylmethionine Decarboxylase
Polyamines
Genes
Fusion reactions
Spermidine
glutathionylspermidine synthetase
Biosynthesis
Membrane Proteins
Enzymes
Bacteria
Bacterial Genomes
Horizontal Gene Transfer
Putrescine
Gene Fusion
Archaea
Gene transfer
Multigene Family
Eukaryota
Patents and inventions

Keywords

  • biosynthesis
  • enzyme activity
  • evolutionary biology
  • genomics
  • metabolism
  • polyamines

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

A polyamine-independent role for S-adenosylmethionine decarboxylase. / Li, Bin; Kurihara, Shin; Kim, Sok Ho; Liang, Jue; Michael, Anthony J.

In: The Biochemical journal, Vol. 476, No. 18, 20.09.2019, p. 2579-2594.

Research output: Contribution to journalArticle

Li, Bin ; Kurihara, Shin ; Kim, Sok Ho ; Liang, Jue ; Michael, Anthony J. / A polyamine-independent role for S-adenosylmethionine decarboxylase. In: The Biochemical journal. 2019 ; Vol. 476, No. 18. pp. 2579-2594.
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