<scp>DmdA</scp> ‐independent lag phase shortening in <i>Phaeobacter inhibens</i> bacteria under stress conditions

Bacteria can shorten their lag phase by using methyl groups from compounds like dimethylsulfoniopropionate (DMSP), which are incorporated into cellular components via the methionine cycle. However, the role of specific methionine synthases in this process is not fully understood. Using transcriptomics, genetics, and biochemical assays, we investigated methionine synthases involved in lag phase shortening in Phaeobacter inhibens. We focused on a cobalamin-dependent methionine synthase (MetH)-like complex encoded by three genes: a betaine-homocysteine S-methyltransferase (bmt), a cobalamin-binding protein (cbp), and an intermediate methyl carrier (PGA1_c16040). Expression profiling revealed transcriptional decoupling among these genes. Deleting bmt disrupted lag phase shortening in response to DMSP. Functional assays showed that Bmt can directly produce methionine from DMSP and betaine, independent of tetrahydrofolate (THF) or cobalamin. Interestingly, under stress conditions, lag phase shortening occurred even in the absence of dimethylsulfoniopropionate demethylase DmdA, the primary DMSP demethylase. Under osmotic and oxidative stress, bmt expression increased significantly in response to both DMSP and betaine, suggesting an alternative methylation route. This highlights the role of Bmt as both demethylase and a methionine synthase under stress, offering a cost-effective strategy for methyl group assimilation. Our findings reveal a novel stress-responsive pathway for methionine synthesis and demonstrate the role of Bmt in promoting bacterial adaptation by accelerating the lag phase.