38. INITIATION OF TRANSLATION Flashcards
1
Q
- What can be said about the translation of all the mRNAs in a cell?
A
- they can be translated simultaneously
2
Q
- What can block the initiation of the translation of selected mRNAs?
A
- regulatory proteins
- they bind to sequences or structures
- they bind within the untranslated 5’ region of the
mRNA - this prevents the attachment of the Ribosomes to the
mRNA
THIS CAN ALSO BE CAUSED BY:
- Non-Coding RNA
3
Q
- What are the 4 aspects of Protein Processing that exist to produce functional proteins?
A
- Polypeptide Cleavage
- Protein Folding
- Subunit Assembly
- Chemical Modifications
4
Q
- What is Polypeptide Cleavage?
A
- some polypeptides are activated by enzymes that
cleave them - this happens in the Rough Endoplasmic Reticulum
- EG: insulin
5
Q
- What is Protein Folding?
A
- this achieves the tertiary structure of the protein
- it is the formation of disulphide bonds
- this happens in the Rough Endoplasmic Reticulum
6
Q
- What is Subunit Assembly?
A
- this forms the Quaternary protein structure
- some polypeptides will come together as the subunits
of a functional protein - this happens in the Rough endoplasmic Reticulum
- EG: Haemoglobin
7
Q
- What is Chemical Modification?
A
- this is the addition of chemical groups to the proteins
- this forms glycoproteins
- this forms lipoproteins
- some of this happens in the Golgi
- most of this happens in the Rough Endoplasmic
Reticulum
8
Q
- What is Protein Degradation?
A
- this marks a particular protein for destruction
- the cell attaches the protein to Ubiquitin (protein)
- non-functional and mis-folded proteins are also
attached to the Ubiquitin
9
Q
- What happens to the Ubiquitinated Proteins?
A
- they are targeted by the Proteasome
- this degrades them
10
Q
- What are Proteasomes?
A
- they are giant protein complexes
- they are 26 S
- they bind to protein molecules
- they degrade them
11
Q
- What happens to long lived proteins?
A
- they are degraded in the Lysosome