Protein Biosynthesis

BCH440H (BCH1440H)

“The life of proteins: from birth to death”

This course is presented as eight themes.

  1. Structure, assembly, and evolution of the ribosome.
  2. mRNA synthesis, maturation, and localization.
  3. Mechanisms and regulation of translation initiation.
  4. Fidelity during translation elongation.
  5. Translation termination and translation-mediated mRNA decay
  6. Nascent protein folding and molecular chaperones.
  7. Protein degradation via the ubiquitin proteasome system and autophagy.
  8. Protein aging, misfolding and disease.

In addition to the lectures, students will work in groups during tutorial sessions to interpret a recent paper related to one of the eight themes to be formally presented during regular class hours.

Bacterial Ribosome

Course Next Offered

January 2019

Course Time and Location

Tuesday and Thursday, 9 to 10 AM
Room 4279, Medical Sciences Building

Prerequisites

BCH210H1/BCH242Y1;BCH311H1/MGY311Y1/CSB349H1/PSL350H1

Enrollment Limit

Yes — 45

Method of Student Evaluation

Midterm Exam (Themes 1 to 4) 30%
Final Exam (Themes 5 to 8) 30%
Student Group Presentations (2 x 14%) 28%
Critical Reflection Papers (6 X 2%) 12%

Presentations/Critical Reflection Papers

A recent high-profile scientific paper related to each of the eight course themes will be assigned to be read, analyzed and presented in class by students working in groups. These talks will be graded based on the quality of background information, explanation of methodology, interpretation of results, and ability to respond to audience questions. This task is expected require significant effort.

Students not involved in presenting the paper will still be required to read the paper and write a 500-word “critical reflection paper”. This is not the same as a rigorous scientific critique. Instead the student is expected to report how the paper contributes to their learning relative to previous experience and their understanding of the course themes. Details will be given at the beginning of the term. Each paper will be assigned two weeks in advance of the due date for presentations/critical reflection paper deadline. This task will require much less effort than a scientific critique and this is reflected in the grading scheme.

 

Course Related News

New therapeutic opportunity for the treatment of resistant malignant melanoma
https://www.sciencedaily.com/releases/2018/06/180620150120.htmResearchers have revealed that malignant melanoma can reprogram their protein synthesis machinery and become addicted to a new family of enzymes that modify transfer RNAs during acquired resistance. The inhibition of these molecules synergies with targeted therapies to produce a strong anti-tumoral effect. These new findings will be key in the development of improved diagnostic tools and melanoma treatment.
Structural biology: Until the last cut
https://www.sciencedaily.com/releases/2018/06/180612185107.htmRibosomes are the cell’s protein factories. Researchers have now structurally characterized late stages in the assembly of the human small ribosomal subunit, yielding detailed insights into their maturation principles.
Cellular ‘garbage disposal’ has another job
https://www.sciencedaily.com/releases/2018/07/180710101708.htmResearchers have found that the cellular ‘garbage disposal,’ known to scientists as proteasomes, may not only be responsible for the removal of cellular waste, but actually work on some of the most important proteins to neuronal development.
Longer-lived animals have longer-lived proteins
https://www.sciencedaily.com/releases/2018/02/180213154958.htmResearchers studying half-lives of evolutionarily related proteins in different species uncovered a link between species lifespan and protein lifespan.
Chaperones can hold proteins in non-equilibrium states
https://www.sciencedaily.com/releases/2018/03/180305130219.htmChaperones are specialized proteins in the cell that help other proteins to reach their functional 3D shapes, which correspond to the states preferred at thermodynamic equilibrium. But a new study shows that chaperones can also maintain proteins in non-equilibrium states, potentially altering their fate.
Researchers discover system that could reduce neurodegeneration in Huntington’s disease: Mechanism could reduce the toxic aggregation of huntingtin protein in the long run
https://www.sciencedaily.com/releases/2018/07/180726161058.htmNeuroscientists have made an important step towards understanding the mechanisms that cause the neurodegenerative disorder Huntington’s disease. Particularly, they identified a system blocking the accumulation of toxin protein aggregates, which are responsible for neurodegeneration.

Coordinator

John R. Glover

John R. Glover

Rm 1616 MaRS West Tower
416-200-5985
john.glover@utoronto.ca

Instructors

Last Updated 20 August 2018