Role of and Long-Chain Acyl-CoA Synthetase FadD in Long-Term Survival

Overview

Journal Microorganisms

Specialty Microbiology

Date 2020 Apr 1

PMID 32225039

Citations 5

Authors

Angel de la Cruz Pech-Canul

Geovanny Rivera-Hernandez

Joaquina Nogales

Otto Geiger

Maria J Soto

Isabel M Lopez-Lara

Affiliations

Soon will be listed here.

Abstract

FadD is an acyl-coenzyme A (CoA) synthetase specific for long-chain fatty acids (LCFA). Strains mutated in fadD cannot produce acyl-CoA and thus cannot grow on exogenous LCFA as the sole carbon source. Mutants in the fadD (smc02162) of Sinorhizobium meliloti are unable to grow on oleate as the sole carbon source and present an increased surface motility and accumulation of free fatty acids at the entry of the stationary phase of growth. In this study, we found that constitutive expression of the closest FadD homologues of S. meliloti, encoded by sma0150 and smb20650, could not revert any of the mutant phenotypes. In contrast, the expression of Escherichia coli fadD could restore the same functions as S. meliloti fadD. Previously, we demonstrated that FadD is required for the degradation of endogenous fatty acids released from membrane lipids. Here, we show that absence of a functional fadD provokes a significant loss of viability in cultures of E. coli and of S. meliloti in the stationary phase, demonstrating a crucial role of fatty acid degradation in survival capacity.

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