otro2 Flashcards
Where does translation start in prokaryotes and eukaryotes? Describe the process.
The ribosome attaches its two units to the
mRNA and begins to read it from the 5’ to the 3’ end until it reaches the start codon ( AUG,GUG,UUG) ( AUG Met)
The start codon is preceded by a whole initiation complex , in the middle of which is a purine-rich sequence :
ÿ Prokaryotes: Shine-Dalgarno sequence
ÿ Eukaryotes: Kozak sequence
Name at least two antibiotics and/or toxins that inhibit protein synthesis and briefly describe the mechanism.
Streptomycin: inhibits initiation (inhibits binding of fMet-rTRNA) and thus causes a
incorrect reading of mRNA
Tetracycline: binds to the 30 subunit and inhibits the attachment of the aminoacyl-tRNA
What is the typical structure of eukaryotic transcription factors? Name three typical DNA binding structures.
Transcription factors bind to specific sections of DNA and regulate how much messenger RNA (mRNA) is produced
from it (transcription rate).
1.DNA-binding domain:
2.Activation domain: initiates transcription through interactions with RNA Pol II and/or its associated proteins or
through local changes in chromatin structure
DNA-binding structures in eukaryotic transcription factors:
-* Homeodomain (helix-turn-helix)
* Leucine zipper domain (bZip domain)
* Zinc finger domains
The binding of oxygen depends on the oxygen partial pressure:
- high O2 partial pressure: protein is oxygenated > R-form
- low O2 partial pressure, no O2 bound > T-shape
e Bohr effect
describes the decrease in the affinity of hemoglobin (Hb) to oxygen when the pH value decreases
or the CO2 concentration increasesThe lower the pH value, the easier H+ is absorbed and O2 is released.
Types of enzyme regulation: Explain how the enzymatic activity of proteins can be regulated. Give one
example of each.
- Allosterische Regulation - Aspartat Transcarbamoylase
Activator molecules occupy the allosteric center and thus cause a conformational
change: - Regulation with Isoenzyme - LDH-Formen: M4-Isoenzym, H4-Isoenzym
- Regulation by covalent modification - histones in DNA packaging
- Activation by proteolytic cleavage - pepsin in the stomach, trypsin in the pancreas
- Activation by co-activators – CoA, metal ions