Tracey Gloster

Last updated
Tracey Gloster
Born
Tracey Maureen Gloster
Alma mater University of Warwick (BSc)
University of York (PhD)
Scientific career
Fields Structural biology
Chemical biology
Glycobiology
Carbohydrate processing enzymes [1]
Institutions University of St Andrews
Simon Fraser University
Thesis Transition state mimicry in glycoside hydrolysis  (2005)
Doctoral advisor Gideon Davies [2]
Website risweb.st-andrews.ac.uk/portal/en/persons/tracey-gloster(d02c38ef-6020-455d-8ec5-d72eeb81ad64).html OOjs UI icon edit-ltr-progressive.svg

Tracey Maureen Gloster is a chemist at the University of St Andrews UK. [1] [3] Her research interests are in structural biology, chemical biology, glycobiology and carbohydrate processing enzymes. [1]

Contents

Education

Gloster studied biochemistry at University of Warwick, graduating in 2002 [4] and then moved to University of York where she was awarded a PhD in chemistry in 2005 for research supervised by Gideon Davies. [2] [5]

Career and research

In her early career she was funded by the Wellcome Trust, initially with a Henry Wellcome post-doctoral fellowship held between 2008 and 2011 at Simon Fraser University, Canada, where she worked with David Vocadlo, [4] [6] and then a Wellcome Trust Research Career Development fellowship in 2012 when she joined the University of St Andrews, Scotland. As of 2022 she holds the position of Reader. [7]

Her research is about all aspects of enzymes that deal with carbohydrates within eukaryotes. [7] Carbohydrates are made from a very wide range of sugar molecules that can be attached to each and other molecules in diverse ways. These glycosylations can have profound consequences for the roles and activities of the molecules and can result in disease if the cell does not process them correctly. Identifying the location and nature of glycosylations is technically challenging, in addition to the challenge of linking them to functions. Gloster has applied inhibitors to gain more understanding about exactly how they work, including describing a new class of glycosyltransferase inhibitors. [5] The techniques that Gloster uses includes ones based around cells, including molecular biology and cell cultures, as well as biophysical methods such as enzyme kinetics, X-ray crystallography and isothermal titration calorimetry. [8]

Publications

Gloster is the author or co-author of over 50 scientific publications. [1] [3] They include:

Awards and honours

Gloster was awarded the Biochemical Society early career research award in 2012, [15] the L’Oreal UK and Ireland Fellowship For Women In Science Fellowship in 2013 [7] and she was awarded the Dextra Medal by the Royal Society of Chemistry in 2019 for her work in carbohydrate chemistry largely conducted in the UK within 15 years of gaining a PhD.

She serves as a member of the Royal Society International Exchanges Committee between 2017 - 2022. [16] She serves as treasurer of the Royal Society of Chemistry Carbohydrate Interest Group. [17] She chairs one of the review panels that judge requests to use the Diamond Light Source. [18]

She is a member of the Young Academy of Scotland. [7]

Related Research Articles

A glycosidic bond or glycosidic linkage is a type of covalent bond that joins a carbohydrate (sugar) molecule to another group, which may or may not be another carbohydrate.

Glycosylation is the reaction in which a carbohydrate, i.e. a glycosyl donor, is attached to a hydroxyl or other functional group of another molecule in order to form a glycoconjugate. In biology, glycosylation usually refers to an enzyme-catalysed reaction, whereas glycation may refer to a non-enzymatic reaction. Glycosylation is a form of co-translational and post-translational modification. Glycans serve a variety of structural and functional roles in membrane and secreted proteins. The majority of proteins synthesized in the rough endoplasmic reticulum undergo glycosylation. Glycosylation is also present in the cytoplasm and nucleus as the O-GlcNAc modification. Aglycosylation is a feature of engineered antibodies to bypass glycosylation. Five classes of glycans are produced:

Glycosyltransferase Class of enzymes that catalyze the transfer of glycosyl groups to an acceptor

Glycosyltransferases are enzymes that establish natural glycosidic linkages. They catalyze the transfer of saccharide moieties from an activated nucleotide sugar to a nucleophilic glycosyl acceptor molecule, the nucleophile of which can be oxygen- carbon-, nitrogen-, or sulfur-based.

CAZy is a database of Carbohydrate-Active enZYmes (CAZymes). The database contains a classification and associated information about enzymes involved in the synthesis, metabolism, and recognition of complex carbohydrates, i.e. disaccharides, oligosaccharides, polysaccharides, and glycoconjugates. Included in the database are families of glycoside hydrolases, glycosyltransferases, polysaccharide lyases, carbohydrate esterases, and non-catalytic carbohydrate-binding modules. The CAZy database also includes a classification of Auxiliary Activity redox enzymes involved in the breakdown of lignocellulose.

Glycoside hydrolase family 2

In molecular biology, Glycoside hydrolase family 2 is a family of glycoside hydrolases.

Glycoside hydrolase family 25

In molecular biology, glycoside hydrolase family 25 is a family of glycoside hydrolases.

Glycoside hydrolase family 31

In molecular biology, glycoside hydrolase family 31 is a family of glycoside hydrolases.

Glycoside hydrolase family 32 Family of glycoside hydrolases

In molecular biology, glycoside hydrolase family 32 is a family of glycoside hydrolases.

Glycoside hydrolase family 4

In molecular biology, glycoside hydrolase family 4 is a family of glycoside hydrolases.

Glycoside hydrolase family 49

In molecular biology, glycoside hydrolase family 49 is a family of glycoside hydrolases.

Glycoside hydrolase family 56

In molecular biology, glycoside hydrolase family 56 is a family of glycoside hydrolases.

In molecular biology, glycoside hydrolase family 63 is a family of glycoside hydrolases.

Glycoside hydrolase family 27

In molecular biology, glycoside hydrolase family 27 is a family of glycoside hydrolases.

In molecular biology, glycoside hydrolase family 37 is a family of glycoside hydrolases.

In molecular biology, glycoside hydrolase family 101 is a family of glycoside hydrolases.

In molecular biology, glycoside hydrolase family 44 is a family of glycoside hydrolases.

In molecular biology, glycoside hydrolase family 89 is a family of glycoside hydrolases.

Protein <i>O</i>-GlcNAcase

Protein O-GlcNAcase (EC 3.2.1.169, OGA, glycoside hydrolase O-GlcNAcase, O-GlcNAcase, BtGH84, O-GlcNAc hydrolase) is an enzyme with systematic name (protein)-3-O-(N-acetyl-D-glucosaminyl)-L-serine/threonine N-acetylglucosaminyl hydrolase. OGA is encoded by the MGEA5 gene. This enzyme catalyses the removal of the O-GlcNAc post-translational modification in the following chemical reaction:

  1. [protein]-3-O-(N-acetyl-β-D-glucosaminyl)-L-serine + H2O ⇌ [protein]-L-serine + N-acetyl-D-glucosamine
  2. [protein]-3-O-(N-acetyl-β-D-glucosaminyl)-L-threonine + H2O ⇌ [protein]-L-threonine + N-acetyl-D-glucosamine
Gideon Davies Professor of Chemistry

Gideon John Davies is a Professor of Chemistry in the Structural Biology Laboratory (YSBL) at the University of York, UK. Davies is best known for his ground-breaking studies into carbohydrate-active enzymes, notably analysing the conformational and mechanistic basis for catalysis and applying this for societal benefit. In 2016 Davies was apppointed the Royal Society Ken Murray Research Professor at the University of York.

Barbara Imperiali is a Professor of Biology and Chemistry at Massachusetts Institute of Technology and Affiliate Member of the Broad Institute. She is an elected member of the National Academy of Sciences and a Fellow of the Royal Society of Chemistry.

References

  1. 1 2 3 4 Tracey Gloster publications indexed by Google Scholar OOjs UI icon edit-ltr-progressive.svg
  2. 1 2 Gloster, Tracey Maureen (2005). Transition state mimicry in glycoside hydrolysis. york.ac.uk (PhD thesis). The University of York. OCLC   1063339504. EThOS   uk.bl.ethos.533533.
  3. 1 2 Tracey Gloster publications from Europe PubMed Central
  4. 1 2 "User:Tracey Gloster". cazypedia.org. CAZypedia: carbohydrate active enzymes. Retrieved 2 September 2020.
  5. 1 2 "Early Career Research Awards – researchers within 5 years of their PhD: Molecular Structure and Function Dr Tracey Gloster" (PDF). portlandpress.com. Portland Press . Retrieved 2 September 2020.
  6. ↑ "Dissection of O-glycosylation of nuclear and cytoplasmic proteins". wellcome.ac.uk. The Wellcome Trust. Retrieved 3 September 2020.
  7. 1 2 3 4 "Tracey Gloster". youngacademyofscotland.org.uk. RSE Young Academy of Scotland. Retrieved 2 September 2020.
  8. ↑ "Tracey Gloster". st-andrews.ac.uk. University of St Andrews. Retrieved 3 September 2020.
  9. ↑ Januka S Athukoralage; Stephen A McMahon; Changyi Zhang; et al. (15 January 2020). "An anti-CRISPR viral ring nuclease subverts type III CRISPR immunity". Nature . 577 (7791): 572–575. doi:10.1038/S41586-019-1909-5. ISSN   1476-4687. PMC   6986909 . PMID   31942067. Wikidata   Q92669532.
  10. ↑ Tracey M Gloster (20 March 2020). "Exploitation of carbohydrate processing enzymes in biocatalysis". Current Opinion in Chemical Biology. 55: 180–188. doi:10.1016/J.CBPA.2020.01.015. ISSN   1367-5931. PMID   32203896. Wikidata   Q90594642.
  11. ↑ Weiwu Ren; Robert Pengelly; Marco Farren-Dai; et al. (13 August 2018). "Revealing the mechanism for covalent inhibition of glycoside hydrolases by carbasugars at an atomic level". Nature Communications . 9 (1): 3243. doi:10.1038/S41467-018-05702-7. ISSN   2041-1723. PMC   6089974 . PMID   30104598. Wikidata   Q58786771. (erratum)
  12. ↑ Laura Griffin; Tracey Gloster (24 July 2017). "The Enzymatic Degradation of Heparan Sulfate". Protein and Peptide Letters. doi:10.2174/0929866524666170724113452. ISSN   0929-8665. PMID   28741461. Wikidata   Q39456712.
  13. ↑ Tracey M Gloster (19 September 2014). "Advances in understanding glycosyltransferases from a structural perspective". Current Opinion in Structural Biology. 28: 131–141. doi:10.1016/J.SBI.2014.08.012. ISSN   0959-440X. PMC   4330554 . PMID   25240227. Wikidata   Q38252791.
  14. ↑ Tracey M Gloster; David J Vocadlo (18 July 2012). "Developing inhibitors of glycan processing enzymes as tools for enabling glycobiology". Nature Chemical Biology . 8 (8): 683–694. doi:10.1038/NCHEMBIO.1029. ISSN   1552-4450. PMID   22810773. Wikidata   Q38027408.
  15. ↑ "2012 Award Winners". biochemistry.org. The Biochemical Society. Retrieved 2 September 2020.
  16. ↑ "Tracey Gloster". royalsociety.org. The Royal Society. Retrieved 2 September 2020.
  17. ↑ "Carbohydrate Group". rsc.org. Royal Society of Chemistry. Retrieved 2 October 2020.
  18. ↑ "Apply for Beamtime - Peer Review". diamond.ac.uk. Retrieved 2 September 2020.
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