1. Post Translational Modification Zachry Theis Clarity Argall

2. Overview • Post Translational Modification • Glycosylation • Tyrosine Sulfonation

3. Glycosylation • Description • Purpose of Glycosylation • Mechanism • Types of Glycosylation

4. Description • Post Translational Modification • Enzymatic Process • Carbohydrate Attachment • Found frequently in ER and golgi

5. Structural Components Protein Folding Specific Recognition Endogeneous Recogoniton Exogeneous Recognition Purpose

6. Mechanism • α linkage • β linkage

7. N-Linked O-linked C-Linked Types of Glycosylation • Glycation

8. N-Linked • Largely In Eukaryotes • Addition to Asparagine • Oligosaccharyltransferase • High Mannose Oligosaccharides • Complex Oligosaccharides

9. O-Linked • After N-glycosylation • Golgi • Serine and Threonine • UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase

10. C-Linked • Mannose to Tryptophan • Less common • Thrombospondins

11. Glycation • Non Enzymatic • Endogeneous or Exogeneous • Impairs function • Alzheimer’s and Parkinson

12. Tyrosine Sulfation

13. Tyrosine Sulfation • Posttranslational Modification • Sulfate group added to Tyrosine residue of protein • Occurs in Golgi Apparatus Tyrosine

14. Tyrosylprotein sulfotransferase Catalyst

15. Mechanism

16. 3'-Phosphoadenosine-5'-phosphosulfate

17. Function • Strengthens Protein-Protein Interactions • Examples: • Serine Protease Inhibitors • Adhesion Molecules • Coagulation Factors

18. References Alberts, Bruce. Molecular Biology of the Cell. New York: Garland Science, 2008. Print "Glycosylation." UniProt. UniProt, 20 July 2011. Web. 19 Nov. 2011. <http://www.uniprot.org/manual/carbohyd>. Varki, Ajit. Essentials of Glycobiology. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory, 2009. Print