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Phosphorylation and sulfation share a common biosynthetic pathway, but extend biochemical and evolutionary diversity of biological macromolecules in distinct ways

Andrade De Lima, Marcelo; Rudd, TR; Fernig, DG; Yates, EA

Phosphorylation and sulfation share a common biosynthetic pathway, but extend biochemical and evolutionary diversity of biological macromolecules in distinct ways Thumbnail


Authors

TR Rudd

DG Fernig

EA Yates



Abstract

<jats:p>Phosphate and sulfate groups are integral to energy metabolism and introduce negative charges into biological macromolecules. One purpose of such modifications is to elicit precise binding/activation of protein partners. The physico-chemical properties of the two groups, while superficially similar, differ in one important respect—the valency of the central (phosphorus or sulfur) atom. This dictates the distinct properties of their respective esters, di-esters and hence their charges, interactions with metal ions and their solubility. These, in turn, determine the contrasting roles for which each group has evolved in biological systems. Biosynthetic links exist between the two modifications; the sulfate donor 3′-phosphoadenosine-5′-phosphosulfate being formed from adenosine triphosphate (ATP) and adenosine phosphosulfate, while the latter is generated from sulfate anions and ATP. Furthermore, phosphorylation, by a xylosyl kinase (Fam20B, glycosaminoglycan xylosylkinase) of the xylose residue of the tetrasaccharide linker region that connects nascent glycosaminoglycan (GAG) chains to their parent proteoglycans, substantially accelerates their biosynthesis. Following observations that GAG chains can enter the cell nucleus, it is hypothesized that sulfated GAGs could influence events in the nucleus, which would complete a feedback loop uniting the complementary anionic modifications of phosphorylation and sulfation through complex, inter-connected signalling networks and warrants further exploration.</jats:p>

Citation

Andrade De Lima, M., Rudd, T., Fernig, D., & Yates, E. (2022). Phosphorylation and sulfation share a common biosynthetic pathway, but extend biochemical and evolutionary diversity of biological macromolecules in distinct ways. Journal of the Royal Society. Interface, 19(193), https://doi.org/10.1098/rsif.2022.0391

Journal Article Type Article
Acceptance Date Jun 11, 2022
Online Publication Date Aug 3, 2022
Publication Date 2022-08
Publicly Available Date May 30, 2023
Journal Journal of the Royal Society Interface
Print ISSN 1742-5689
Electronic ISSN 1742-5662
Publisher The Royal Society
Peer Reviewed Peer Reviewed
Volume 19
Issue 193
DOI https://doi.org/10.1098/rsif.2022.0391
Publisher URL https://royalsocietypublishing.org/doi/10.1098/rsif.2022.0391

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