Distinct roles of the N- and C-terminal regions of MetW in MetX interaction and activation in Pseudomonas aeruginosa

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ID: 337474
2026
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Abstract
In methionine biosynthesis, homoserine O-acylation is catalyzed by MetX together with its regulatory protein, MetW, in some bacteria. MetW interacts with MetX and regulates its enzymatic activity. Although this interaction and regulation are likely indispensable for efficient methionine biosynthesis, the specific regions of MetW crucial for these functions remain unidentified. Here, we characterize this system using MetW and MetX from Pseudomonas aeruginosa (PaMetW and PaMetX, respectively). We found that the N-terminal region of PaMetW and the C-terminal region of PaMetX are critical for their interaction. Additionally, the C-terminal region of PaMetW is essential for enhancing homoserine O-succinylation activity. Structural models predict that the PaMetW N-terminal region is located near the PaMetX C-terminal region and that the two terminal regions form an intermolecular parallel β-sheet. These results suggest that the N- and C-terminal regions of PaMetW play important roles in the interaction with PaMetX and enhancement of its enzymatic activity, respectively.
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openalex_W7223984022 Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Fumihito Hasebe, Chitose Maruyama, Yoshimitsu Hamano
Journal bioscience biotechnology and biochemistry
Year 2026
DOI
10.1093/bbb/zbag162
URL
https://doi.org/10.1093/bbb/zbag162
Keywords Keywords not found

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