Post Translational Modification Zachry Theis Clarity Argall

Overview Post Translational Modification Glycosylation Tyrosine Sulfonation

Glycosylation Description Purpose of Glycosylation Mechanism Types of Glycosylation

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

Purpose Structural Components Specific Recognition Protein Folding Endogeneous Recogoniton Exogeneous Recognition

Mechanism α linkage β linkage

Types of Glycosylation N-Linked O-linked C-Linked Glycation

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

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

C-Linked Mannose to Tryptophan Less common Thrombospondins

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

Tyrosine Sulfation

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

Tyrosylprotein sulfotransferase Catalyst

Mechanism

3'-Phosphoadenosine-5'-phosphosulfate

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

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