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- W4281845900 endingPage "669" @default.
- W4281845900 startingPage "656" @default.
- W4281845900 abstract "Polysaccharide methylation, especially that of pectin, is a common and important feature of land plant cell walls. Polysaccharide methylation takes place in the Golgi apparatus and therefore relies on the import of S-adenosyl methionine (SAM) from the cytosol into the Golgi. However, so far, no Golgi SAM transporter has been identified in plants. Here we studied major facilitator superfamily members in Arabidopsis that we identified as putative Golgi SAM transporters (GoSAMTs). Knockout of the two most highly expressed GoSAMTs led to a strong reduction in Golgi-synthesized polysaccharide methylation. Furthermore, solid-state NMR experiments revealed that reduced methylation changed cell wall polysaccharide conformations, interactions and mobilities. Notably, NMR revealed the existence of pectin ‘egg-box’ structures in intact cell walls and showed that their formation is enhanced by reduced methyl esterification. These changes in wall architecture were linked to substantial growth and developmental phenotypes. In particular, anisotropic growth was strongly impaired in the double mutant. The identification of putative transporters involved in import of SAM into the Golgi lumen in plants provides new insights into the paramount importance of polysaccharide methylation for plant cell wall structure and function. Polysaccharide methylation, important for cell wall structure and function, occurs in the Golgi and relies on the import of S-adenosyl methionine (SAM) molecules into the Golgi lumen by Golgi SAM transporters. This work shows the discovery and relevance of putative SAM transporters." @default.
- W4281845900 created "2022-06-13" @default.
- W4281845900 creator A5001375415 @default.
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- W4281845900 date "2022-06-09" @default.
- W4281845900 modified "2023-10-15" @default.
- W4281845900 title "Golgi-localized putative S-adenosyl methionine transporters required for plant cell wall polysaccharide methylation" @default.
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