SGNH Hydrolase-Like Proteins AlgJ and AlgX Have Similar Topology but Separate and Distinct Roles in Alginate Acetylation

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Bacteria utilize many defense strategies to protect themselves against external forces. One mechanism used by the bacterium Pseudomonas aeruginosa is the production of the long sugar polymer alginate. The bacteria use this polymer to form a biofilm – a barrier to protect against antibiotics and the host immune response. During its biosynthesis alginate undergoes a chemical modification whereby acetate is added to the polymer. Acetylation of alginate is important as this modification makes the bacterial biofilm less susceptible to recognition and clearance by the host immune system. In this paper we present the atomic structure of AlgJ; one of four proteins required for O-acetylation of the polymer. AlgJ is structurally similar to AlgX, which we have shown previously is also required for alginate acetylation. To understand why both enzymes are required for O-acetylation we functionally characterized the proteins and found that although AlgJ exhibits acetylesterase activity – catalyzing the removal of acetyl groups from a surrogate substrate – it does not bind to short mannuornic acid polymers. In contrast, AlgX bound alginate in a length-dependent manner and was capable of transfering acetate from a surrogate substrate onto alginate. This has allowed us to not only understand how acetate is added to alginate, but increases our understanding of how acetate is added to other bacterial sugar polymers.

Vyšlo v časopise: SGNH Hydrolase-Like Proteins AlgJ and AlgX Have Similar Topology but Separate and Distinct Roles in Alginate Acetylation. PLoS Pathog 10(8): e32767. doi:10.1371/journal.ppat.1004334
Kategorie: Research Article
prolekare.web.journal.doi_sk: https://doi.org/10.1371/journal.ppat.1004334

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