Recapitulating the Structural Evolution of Redox Regulation in Adenosine 5'-Phosphosulfate Kinase from Cyanobacteria to Plants.
作者： Jonathan Herrmann , David Nathin , Soon Goo Lee , Tony Sun , Joseph M. Jez
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摘要: In plants, adenosine 5′-phosphosulfate (APS) kinase (APSK) is required for reproductive viability and the production of 3′-phosphoadenosine (PAPS) as a sulfur donor in specialized metabolism. Previous studies APSK from Arabidopsis thaliana (AtAPSK) identified regulatory disulfide bond formed between N-terminal domain (NTD) cysteine on core scaffold. This thiol switch unique to mosses, gymnosperms, angiosperms. To understand structural evolution redox control APSK, we investigated redox-insensitive cyanobacterium Synechocystis sp. PCC 6803 (SynAPSK). Crystallographic analysis SynAPSK complex with either APS non-hydrolyzable ATP analog or sulfate revealed overall structure enzyme, which lacks NTD found homologs mosses plants. A series engineered variants reconstructed plant APSK. Biochemical analyses SynAPSK, H23C mutant, fused AtAPSK NTD, fusion protein mutation showed that addition cysteines recapitulated thiol-based regulation. These results reveal molecular basis changes leading green lineage cyanobacteria
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