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  • A bacterial light response reveals an orphan desaturase for human plasmalogen synthesis.

A bacterial light response reveals an orphan desaturase for human plasmalogen synthesis.

Science (New York, N.Y.) (2019-10-12)
Aránzazu Gallego-García, Antonio J Monera-Girona, Elena Pajares-Martínez, Eva Bastida-Martínez, Ricardo Pérez-Castaño, Antonio A Iniesta, Marta Fontes, S Padmanabhan, Montserrat Elías-Arnanz
ABSTRACT

Plasmalogens are glycerophospholipids with a hallmark sn-1 vinyl ether bond. These lipids are found in animals and some bacteria and have proposed membrane organization, signaling, and antioxidant roles. We discovered the plasmanylethanolamine desaturase activity that is essential for vinyl ether bond formation in a bacterial enzyme, CarF, which is a homolog of the human enzyme TMEM189. CarF mediates light-induced carotenogenesis in Myxococcus xanthus, and plasmalogens participate in sensing photooxidative stress through singlet oxygen. TMEM189 and other animal homologs could functionally replace CarF in M. xanthus, and knockout of TMEM189 in a human cell line eliminated plasmalogens. Discovery of the human plasmanylethanolamine desaturase will spur further study of plasmalogen biogenesis, functions, and roles in disease.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Octaethylene glycol, ≥95% (oligomer purity)
Sigma-Aldrich
Benzamidine, ≥95.0%
Sigma-Aldrich
Protoporphyrin IX, ≥95%
Sigma-Aldrich
ANTI-FLAG® M2 antibody, Mouse monoclonal, clone M2, purified immunoglobulin (Purified IgG1 subclass), buffered aqueous solution (10 mM sodium phosphate, 150 mM NaCl, pH 7.4, containing 0.02% sodium azide)