Phosphatidylcholine‐deficient suppressor mutant of Sinorhizobium meliloti, altered in fatty acid synthesis, partially recovers nodulation ability in symbiosis with alfalfa (Medicago sativa).

SUMMARY: Rhizobial phosphatidylcholine (PC) is thought to be a critical phospholipid for the symbiotic relationship between rhizobia and legume host plants. A PC‐deficient mutant of Sinorhizobium meliloti overproduces succinoglycan, is unable to swim, and lacks the ability to form nodules on alfalfa (Medicago sativa) host roots. Suppressor mutants had been obtained which did not overproduce succinoglycan and regained the ability to swim. Previously, we showed that point mutations leading to altered ExoS proteins can reverse the succinoglycan and swimming phenotypes of a PC‐deficient mutant. Here, we report that other point mutations leading to altered ExoS, ChvI, FabA, or RpoH1 proteins also revert the succinoglycan and swimming phenotypes of PC‐deficient mutants. Notably, the suppressor mutants also restore the ability to form nodule organs on alfalfa roots. However, nodules generated by these suppressor mutants express only low levels of an early nodulin, do not induce leghemoglobin transcript accumulation, thus remain white, and are unable to fix nitrogen. Among these suppressor mutants, we detected a reduced function mutant of the 3‐hydoxydecanoyl‐acyl carrier protein dehydratase FabA that produces reduced amounts of unsaturated and increased amounts of shorter chain fatty acids. This alteration of fatty acid composition probably affects lipid packing thereby partially compensating for the previous loss of PC and contributing to the restoration of membrane homeostasis. Significance Statement: The membrane lipid phosphatidylcholine (PC) is crucial for the bacterium Sinorhizobium meliloti when generating nitrogen‐fixing nodules on the roots of their host plant. Although PC‐deficient mutants of S. meliloti cannot form any nodules on their host plant, suppressor mutants were isolated which partially recover the ability to trigger nodule formation. Among these suppressor mutants, we detected a reduced function mutant of FabA that produces reduced amounts of unsaturated and increased amounts of shorter chain fatty acids thereby probably affecting lipid packing. [ABSTRACT FROM AUTHOR]