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Updated: May 11, 2026

Sequence-specific Labeling of Nucleic Acids and Proteins with Methyltransferases and Cofactor Analogues
Published on: November 22, 2014
The endosymbiont Amoebophilus asiaticus encodes an S-adenosylmethionine carrier that compensates for its missing
Ilka Haferkamp1, Thomas Penz, Melanie Geier
1Zelluläre Physiologie/Membrantransport, Technische Universität Kaiserslautern, Kaiserslautern, Germany.
Abstract:
All organisms require S-adenosylmethionine (SAM) as a methyl group donor and cofactor for various biologically important processes. However, certain obligate intracellular parasitic bacteria and also the amoeba symbiont Amoebophilus asiaticus have lost the capacity to synthesize this cofactor and hence rely on its uptake from host cells. Genome analyses revealed that A. asiaticus encodes a putative SAM transporter. The corresponding protein was functionally characterized in Escherichia coli: import studies demonstrated that it is specific for SAM and S-adenosylhomocysteine (SAH), the end product of methylation. SAM transport activity was shown to be highly dependent on the presence of a membrane potential, and by targeted analyses, we obtained direct evidence for a proton-driven SAM/SAH antiport mechanism. Sequence analyses suggest that SAM carriers from Rickettsiales might operate in a similar way, in contrast to chlamydial SAM transporters. SAM/SAH antiport is of high physiological importance, as it allows for compensation for the missing methylation cycle. The identification of a SAM transporter in A. asiaticus belonging to the Bacteroidetes phylum demonstrates that SAM transport is more widely spread than previously assumed and occurs in bacteria belonging to three different phyla (Proteobacteria, Chlamydiae, and Bacteroidetes).
Insights
Certain bacteria, like Amoebophilus asiaticus, lack S-adenosylmethionine (SAM) synthesis and use a proton-driven transporter to import SAM, compensating for their lost methylation cycle.
Area of Science:
- Microbiology
- Molecular Biology
- Biochemistry
Background:
- S-adenosylmethionine (SAM) is essential for all organisms as a methyl donor.
- Some parasitic bacteria and amoeba symbionts cannot synthesize SAM and must import it.
- Amoebophilus asiaticus, an amoeba symbiont, was found to lack SAM synthesis capabilities.
Purpose of the Study:
- To identify and functionally characterize the SAM transporter in A. asiaticus.
- To elucidate the mechanism of SAM transport in A. asiaticus.
- To understand the prevalence and evolutionary significance of SAM transport in bacteria.
Main Methods:
- Genome analysis to identify a putative SAM transporter gene in A. asiaticus.
- Heterologous expression and functional characterization of the transporter in Escherichia coli.
- SAM and S-adenosylhomocysteine (SAH) import assays.
- Membrane potential dependency studies and proton-driven antiport mechanism investigation.
Main Results:
- A. asiaticus encodes a specific SAM transporter.
- The transporter mediates the uptake of SAM and SAH, functioning as a SAM/SAH antiporter.
- Transport is driven by a proton gradient, indicating a proton-driven antiport mechanism.
- SAM transport is crucial for compensating the missing methylation cycle in A. asiaticus.
Conclusions:
- The identified SAM transporter in A. asiaticus is vital for its survival by enabling SAM uptake.
- SAM/SAH antiport mechanism is a key strategy for organisms lacking SAM synthesis.
- The presence of SAM transporters in Bacteroidetes expands the known phyla harboring this mechanism, alongside Proteobacteria and Chlamydiae.
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Published on: October 19, 2010
17:12Profiling of Methyltransferases and Other S-adenosyl-L-homocysteine-binding Proteins by Capture Compound Mass Spectrometry (CCMS)
Published on: December 20, 2010
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