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Instruments / Technical Area	Publication Details	Published	Actions
B21-High Throughput SAXS	Centrosome dysfunction associated with somatic expression of the synaptonemal complex protein TEX12 Sumit Sandhu , Ieng F. Sou , Jill E. Hunter , Lucy Salmon , Caroline L. Wilson , Neil D. Perkins , Neil Hunter , Owen R. Davies , Urszula L. Mcclurg Communications Biology 4 DOI: 10.1038/s42003-021-02887-4 Diamond Proposal Number(s): [15836] Open Access Show Abstract ▼ Abstract: The synaptonemal complex (SC) is a supramolecular protein scaffold that mediates chromosome synapsis and facilitates crossing over during meiosis. In mammals, SC proteins are generally assumed to have no other function. Here, we show that SC protein TEX12 also localises to centrosomes during meiosis independently of chromosome synapsis. In somatic cells, ectopically expressed TEX12 similarly localises to centrosomes, where it is associated with centrosome amplification, a pathology correlated with cancer development. Indeed, TEX12 is identified as a cancer-testis antigen and proliferation of some cancer cells is TEX12-dependent. Moreover, somatic expression of TEX12 is aberrantly activated via retinoic acid signalling, which is commonly disregulated in cancer. Structure-function analysis reveals that phosphorylation of TEX12 on tyrosine 48 is important for centrosome amplification but not for recruitment of TEX12 to centrosomes. We conclude that TEX12 normally localises to meiotic centrosomes, but its misexpression in somatic cells can contribute to pathological amplification and dysfunction of centrosomes in cancers.	Dec 2021
I04-1-Macromolecular Crystallography (fixed wavelength) I24-Microfocus Macromolecular Crystallography	Metabolism of multiple glycosaminoglycans by Bacteroides thetaiotaomicron is orchestrated by a versatile core genetic locus Didier Ndeh , Arnaud Basle , Henrik Strahl , Edwin A. Yates , Urszula L. Mcclurgg , Bernard Henrissat , Nicolas Terrapon , Alan Cartmell Nature Communications 11 DOI: 10.1038/s41467-020-14509-4 Diamond Proposal Number(s): [18598] Open Access Show Abstract ▼ Abstract: The human gut microbiota (HGM), which is critical to human health, utilises complex glycans as its major carbon source. Glycosaminoglycans represent an important, high priority, nutrient source for the HGM. Pathways for the metabolism of various glycosaminoglycan substrates remain ill-defined. Here we perform a biochemical, genetic and structural dissection of the genetic loci that orchestrates glycosaminoglycan metabolism in the organism Bacteroides thetaiotaomicron. Here, we report: the discovery of two previously unknown surface glycan binding proteins which facilitate glycosaminoglycan import into the periplasm; distinct kinetic and genetic specificities of various periplasmic lyases which dictate glycosaminoglycan metabolic pathways; understanding of endo sulfatase activity questioning the paradigm of how the ‘sulfation problem’ is handled by the HGM; and 3D crystal structures of the polysaccharide utilisation loci encoded sulfatases. Together with comparative genomic studies, our study fills major gaps in our knowledge of glycosaminoglycan metabolism by the HGM.	Jan 2020

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