3 ECTS credits
75 h study time
Offer 1 with catalog number 4012306ENR for all students in the 2nd semester at a (E) Master - advanced level.
In order to be able to understand the life of proteins, it is a prerequisite to investigate the properties of the cellular environment into which enzymes and other proteins operate. Therefore, this course deals first with the cytoskeleton and the properties of the different elements belonging to this intricate structural network are discussed (microtubule, actin filaments and intermediate filaments). Attention will be paid to the structural organization within the cell.
It will be shown that the intracellular environment clearly differs from the environment in which classically and in vitro enzymes and cellular components are investigated (e.g. in vivo : limitation of diffusion, extreme high protein concentrations in general and, in particular, enzyme concentrations that are higher than their substrates …. This leads to a model in which in vivo enzymes of metabolic pathways are organized in clusters (metabolons). In this respect emphasis is put on the association of proteins to form heterologous protein-protein aggregates. Such interactions are essential not only for the regulation of metabolic pathways (which relies on the formation of metabolons and channeling of metabolites) but for virtually every process taking place in a living cell/organism (e.g. in transcription and translation, signal transduction, in the immune system, during apoptosis, etc..).
The next chapter deals with protein trafficking. It is indeed essential for a cell that newly synthesized proteins are directed towards their correct final destination. Transport of proteins following the general export route via the endoplasmic reticulum and the Golgi apparatus is discussed. The importance of “routing, sorting, retention/salvage and membrane stop-transfer” signals will be explained. The model of cotranslational transport will be extensively discussed of proteins that follow the secretory pathway via the endoplasmatic reticulum (the so-called “signal hypothesis”). In this respect the structure and properties of the signal recognition particle will be explained. In close connection to this issue we look into the different types of protein glycosylation. These co-/post-translational modifications take place when newly synthesized proteins are transported through the ER and the Golgi complex. Next we discuss the import of newly synthesized proteins into eukaryotic subcellular organelles such as mitochondria, chloroplasts, peroxisomes, the nucleus and lysosomes.
Another chapter deals with folding of proteins in the cell. An overview is given of protein disulphide ismoerases and peptidyl prolyl-cis-trans isomerases and of different chaperones and chaperonins that are essential molecules for the in vivo folding of proteins towards their correct three-dimensional structure. Recent structural information on these molecules and on their action is given (e.g. hsp60 with as example GroeL/GroeS, hsp70 with as example dnaJ/dnaK…).
Finally a last chapter describes the degradation of proteins inside the cell, which is a strictly regulated process. We discuss on the structure and the action of the proteasome, which is an essential machinery involved in eukaryotic protein degradation. Attention is paid to the role of ubiquitin in this and in other cellular processes.
All topics dealt with in this course have been amply investigated during recent years, and an overwhelming number of papers and reviews have been published lately.
NA
This course aims to analyze various processes taking place within the living cell.
Students will:
-be able to describe the structural organization of the intracellular components of the cytoskeleton and its associating proteins.
-know and understand the properties of the intracellular environment.
-know and understand the advantages of heterologous protein-protein interactions and of metabolite channeling.
-be able to explain the problem of protein trafficking in the cell in all its aspects.
-know and understand the process of protein folding in the cell.
-be able to describe the process of protein degradation in the cell.
-know and understand the different functions of the protein ubiquitin and of ubiquitin-like molecules.
-be able to make an analysis of different technologies that are used in these domains of research.
The final grade is composed based on the following categories:
Oral Exam determines 80% of the final mark.
SELF Paper determines 20% of the final mark.
Within the Oral Exam category, the following assignments need to be completed:
Within the SELF Paper category, the following assignments need to be completed:
The oral exam of this course consists of two parts:
1. Presentation of one of the general topics, which can be prepared on the basis of two review papers that are provided in advance as well as of the powerpoint slides (1/2 hour)
2. Subsequently a general question related to the course slides will be posed. This question will be provided ¼ hour before the start of the oral exam (1/2 hour).
The evaluation will be done on the oral exam as well as the writing of the paper of the first part of the exam.
The quotation, which is summative, has the following distribution:
1/3 on part 1 of the oral exam
1/3 on part 2 of the oral exam
1/3 on the paper related to part 1
This offer is part of the following study plans:
Master of Bioengineering Sciences: Cell and Gene Biotechnology: Medical Biotechnology (only offered in Dutch)
Master of Bioengineering Sciences: Cell and Gene Biotechnology: Agrobiotechnology (only offered in Dutch)
Master of Bioengineering Sciences: Chemistry and Bioprocess Technology: Food Biotechnology (only offered in Dutch)
Master of Bioengineering Sciences: Chemistry and Bioprocess Technology: Chemical Biotechnology (only offered in Dutch)
Master of Bioengineering Sciences: Chemistry and Bioprocess Technology: Biochemical Biotechnology (only offered in Dutch)
Master of Biomedical Research: Standaard traject