Divergent unsaturated fatty acid synthesis in two highly related model pseudomonads.
Pseudomonas
UFA
desaturase
unsaturated fatty acids
Journal
Molecular microbiology
ISSN: 1365-2958
Titre abrégé: Mol Microbiol
Pays: England
ID NLM: 8712028
Informations de publication
Date de publication:
02 2023
02 2023
Historique:
revised:
15
12
2022
received:
01
11
2022
accepted:
17
12
2022
pubmed:
21
12
2022
medline:
15
3
2023
entrez:
20
12
2022
Statut:
ppublish
Résumé
The genomes of the best-studied pseudomonads, Pseudomonas aeruginosa and Pseudomonas putida, which share 85% of the predicted coding regions, contain a fabA fabB operon (demonstrated in P. aeruginosa, putative in P. putida). The enzymes encoded by the fabA and fabB genes catalyze the introduction of a double bond into a 10-carbon precursor which is elongated to the 16:1Δ9 and 18:1Δ11 unsaturated fatty acyl chains required for functional membrane phospholipids. A detailed analysis of transcription of the P. putida fabA fabB gene cluster showed that fabA and fabB constitute an operon and disclosed an unexpected and essential fabB promoter located within the fabA coding sequence. Inactivation of the fabA fabB operon fails to halt the growth of P. aeruginosa PAO1 but blocks growth of P. putida F1 unless an exogenous unsaturated fatty acid is provided. We report that the asymmetry between these two species is due to the P. aeruginosa PAO1 desA gene which encodes a fatty acid desaturase that introduces double bonds into the 16-carbon acyl chains of membrane phospholipids. Although P. putida F1 encodes a putative DesA homolog that is 84% identical to the P. aeruginosa PAO1, the protein fails to provide sufficient unsaturated fatty acid synthesis for growth when the FabA FabB pathway is inactivated. We report that the P. putida F1 DesA homolog can functionally replace the P. aeruginosa DesA. Hence, the defect in P. putida F1 desaturation is not due to a defective P. putida F1 DesA protein but probably to a weakly active component of the electron transfer process.
Substances chimiques
Fatty Acid Synthase, Type II
EC 6.-
Fatty Acids, Unsaturated
0
Phospholipids
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
252-261Subventions
Organisme : Division of Microbiology and Infectious Diseases, National Institute of Allergy and Infectious Diseases
ID : AI15650
Informations de copyright
© 2022 The Authors. Molecular Microbiology published by John Wiley & Sons Ltd.
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