Protein Biosynthesis -2 By Amr S. Moustafa, M.D.; Ph.D.

Slides:



Advertisements
Similar presentations
The rate of enzyme reactions can be altered during cell metabolism by a number of important methods:- 1.Proteolytic cleavage – enzymes may be kept in an.
Advertisements

Molecular Basis for Relationship between Genotype and Phenotype DNA RNA protein genotype function organism phenotype DNA sequence amino acid sequence transcription.
Gluconeogenesis.
DR AMINA TARIQ BIOCHEMISTRY
Javad Jamshidi Fasa University of Medical Sciences Proteins Into membranes and Organelles and Vesicular Traffic Moving.
Intracellular Compartments
Transport, con't.. The Na/K ATPase Consequences of Na/K ATPase Two ion gradients –Used as energy source –Electrical signaling Charge difference across.
Protein Sorting ISAT 351, Spring 2004 College of Integrated Science and Technology James Madison University.
Relationship between Genotype and Phenotype
Molecular Basis of Peptide Hormone Production
Inside of cell Interior of rough endoplasmic reticulum 5' Receptor protein Signal recognition particle mRNA Ribosome Signal sequence Protein synthesis.
Vesicular Transport III. N-linked glycosylation because sugar is added to N of asparagine. original precursor oligosaccharide added to most proteins in.
O-linkage to GalNAc N-linkage to GlcNAc Posttranslation Modifications 1 Vitamin K-Dependent Modifications Vitamin K is a cofactor in the carboxylation.
Posttranslational modification, folding, assembly, and death 1.Covalent modifications 1)Proteolytic processing: posttranslational processing is called.
Lecture 19-20: Protein Synthesis and the Genetic Code and Synthesis of Membrane Proteins Reading Assignment: Chapter 40 and 43, pgs and ;
Protein synthesis.
Proteolytic Cleavage Removal of the N-terminal methionine and/or other peptides from a proprotein. Acylation The initiator methionine is hydrolyzed and.
REGULATION OF ENZYME ACTIVITY
ROUGH ENDOPLASMIC RETICULUM
Enzyme Biosynthesis Tri Rini Nuringtyas. As we remember ! Most enzymes are proteins so As we remember ! Most enzymes are proteins so Mechanism of enzyme.
Posttranslational Modification of Proteins
CHAPTER 6 SYSTEMS BIOLOGY OF CELL ORGANIZATION
SYNTHESIS OF GLYCOPROTEINS Dr. Nasim AP BIOCHEMISTRY.
Protein folding,maturation & targeting. Secretory pathway: signal peptide recognition.
Posttranslational modification is the chemical modification of a protein after its translationchemical proteintranslation.
Post-Translational Events II ER & Golgi Processes.
Molecular and Cellular Biochemistry 2. ER- protein modifications
8. Protein Synthesis and Protein Processing a). Ribosome structure b). Protein synthesis i). Initiation of protein synthesis ii). Peptide bond formation;
Biosynthesis and degradation of proteins Bruno Sopko.
Cell and Molecular Biology Behrouz Mahmoudi Cell organelles-2 1.
Fates of Proteins in Cells See also pages in Goodman.
Cell Signaling And Hormonal Regulation
Molecular Basis for Relationship between Genotype and Phenotype DNA RNA protein genotype function organism phenotype DNA sequence amino acid sequence transcription.
Regulation of enzyme activity Lecture 6 Dr. Mona A. R.
LEHNINGER PRINCIPLES OF BIOCHEMISTRY
© 2012 Pearson Education, Inc. Lectures by Kathleen Fitzpatrick Simon Fraser University Membranes: Their Structure, Function, and Chemistry Chapter 7.
PROTEINS BIT 230 Biochemistry Purification Characterization.
CHMI E.R. Gauthier, Ph.D. 1 CHMI 2227E Biochemistry I Enzymes: - Regulation.
Regulation of metabolism on the cellular level Vladimíra Kvasnicová.
Biosynthesis and degradation of proteins
 Golgi apparatus or golgi complex or simple Golgi is an organelle found in most of the eukaryotic cells.  It was one of the first organelle to be.
PACKAGING, TRANSPORTING and EXPORTING
Cell Biology Lec.8 Dr: ButhainaAl-Sabawi Date: Cellular Activity protein synthesis: The events involved in gene expression that results in a.
ENDOPLASMIC RETICULUM Submitted by Dr Madhurima Sharma.
Bruno Sopko.  Proteosynthesis  Post-translation processing of proteins  Protein degradation.
4-1 Protein Synthesis Is a Major Function of Cells.
Post-Translational Events I Protein Trafficking
20.4 Regulation of Enzyme Activity
Preparing for the Exam Question 1:  Amino acid structures and abbreviations. Question 2:  Mechanism of trypsin. Question 3:  Serine protease evolution.
Protein Synthesis (Translation)
The Cytomembrane System
Glycogen Metabolism By Dr. Amr S. Moustafa, MD, PhD.
Post Translational Modifications of Proteins
Cytosol Nucleus Mitochondria Secreted ER Golgi Endosome Lysosome Transmembrane.
Chapter 11 Cell Communication.
DNA Translation. DNA Translation Learning Objectives Student will be able to Discuss DNA Translation Explain Post Translational Modifications Solve.
Post-translational Modifications
Major Modes of Activity Regulation
Organelles involved in synthesis and secretion of proteins
Genetic code and Post translational modifications
Enzyme Regulation.
Termination of Translation
Relationship between Genotype and Phenotype
Lizabeth Allison Ch:14 Waever Ch 17, 18, 19
بسم الله الرحمن الرحيم.
Post-Translational Modification
Relationship between Genotype and Phenotype
Philip Cohen, Marianna Tcherpakov  Cell 
Volume 104, Issue 4, Pages (February 2001)
Cell Communication.
Presentation transcript:

Protein Biosynthesis -2 By Amr S. Moustafa, M.D.; Ph.D.

Polyribosome (Polysomes) Several ribosomes and one mRNA

Protein Targeting Free Vs attached ribosomes Localization signals

Regulation of Translation The dephosphorylated eIF: Active form Heme prevents eIF phosphorylation Heme stimulates translation Proteins/mRNA interactions: e.g., Ferritin and transferrin receptor synthesis

Posttranslational Modifications  Trimming  Covalent modifications: PhosphorylationBiotinylation GlycosylationFarnesylation HydroxylationAcetylation Carboxylation  Ubiquitination

Posttranslational Modifications: Trimming  Removal of a part of the translated sequence  Proteases protein activation  Cellular site of cleavage: ER and Golgi apparatus Secretory vesicles: e.g., insulin After secretion: e.g., collagen At sites of action: zymogen e.g., trypsinogen

Posttranslational Modifications: Phosphorylation Addition of phosphate to hydroxyl group of Serine and threonine Tyrosine Reversible: Addition by kinases Removal by phosphatases Increase or decrease the activity of a specific protein e.g., Glycogen synthase and glycogen phosphorylase

Posttranslational Modifications: Phosphorylation

Posttranslational Modifications: Glycosylation Modifications of : proteins of plasma membrane proteins of lysosome secretory proteins Addition of carbohydrate chains to: Hydroxyl group of serine or threonine (O-linked) Amide group of asparagine (N-linked) Site: Golgi apparatus and ER Protein targeting: e.g., mannose-6-phosphate to lysosomal enzymes

Posttranslational Modifications: Glycosylation

Posttranslational Modifications: Hydroxylation Proline and lysine Endoplasmic reticulum Prolyl or lysyl hydroxylases e.g., Collagen

Posttranslational Modifications: Other Covalent Alterations - 1 Carboxylation: γ-carboxylation of glutamic acid residue for maturation of vitamin K-dependent clotting factors II, VII, IX and X

Carboxylation

Posttranslational Modifications: Other Covalent Alterations - 2 Biotinylation Farnesylation e.g., Acetyl Co-A Carboxylase e.g., Protein anchoring to membranes

Posttranslational Modifications: Ubiquitination Proteins: Defective Rapid turnover Ubiquitin: Small, highly conserved protein Proteasome: Complex proteolytic system ATP-dependent Cytosol