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[P01-052]Impact of interaction between homocysteine synthase and sulfur carrier protein upon methionine biosynthesis in Streptomyces albulus

○Maria Igarashi1, Chitose Maruyama1, Yoshimitsu Hamano1, Fumihito Hasebe1 (1. Fukui Prefectural University (Japan))
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Keywords:

methionine biosynthesis,protein-protein interaction,sulfur carrier protein,Streptomyces

Methionine is an essential sulfur-containing amino acid used in protein synthesis. Recently, our group reported the identification of a novel gene (metM) responsible for methionine biosynthesis in Streptomyces albulus NBRC 14147 and demonstrated that the gene product, MetM, is a novel homocysteine synthase using a sulfur carrier protein (MetO) [1]. Although the interaction between MetM and post-translationally modified MetO (MetO-ΔC-thiocarboxylate) should be crucial for the homocysteine synthase activity, there is no knowledge of the interaction. Thus, in this study, we investigate the interaction regions between MetM and MetO, as well as the biological significance of this interaction.
To find interaction-region candidates, we generated a MetM and MetO-ΔC complex model using ColabFold. This complex model suggests that MetM contains four amino-acid residues that should be involved in electrostatic interactions with the globular domain of MetO-ΔC. Then, to evaluate whether these residues are essential for the interaction, we conducted pull-down assays and growth tests. In this presentation, we will report those results.

Reference
[1]F. Hasebe et al. Appl. Environ. Microbiol. 90, e01247-24 (2024).

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