Translation Flashcards
nonsense mutation
stop codon causes truncation of protein, length of mRNA stays the same
only step of translation that requires ATP
charging tRNA with its amino acid!
aminoacyl-tRNA synthetase uses ATP
aminoacyl-tRNA synthetase
enzyme that adds amino acids to tRNA using ATP.
Only step of translation with proofreading, and only step of translation that requires ATP.
only step of translation that requires GTP
moving the charged AA-tRNA into A site
1st codon in proks
formylated, tRNA-F-met
1st codon in euks
tRNA-i-met (i for initiator)
initiation in proks
16S rRNA binds Shine-Dalgarno sequence putting tRNA-F-met in P site
initiation in euks
initiator proteins scan mRNA for Kozak sequence, 40/60S subunits bind and tRNA-i-met is put in P position
mutations in Kozak sequence
translational inefficiency because the ribosomal complex can’t find the initiator proteins as well, ex: beta thalassemia minor
global regulation of protein synthesis
(eiFs) eukaryotic initiation factors that increase protein synthesis, ex: stimulated by ER stress or insulin
eiF2
represses protein synthesis when phosphorylated on alpha subunit, which blocks GDP-GTP conversion. Phosphorylation occurs when cell is under stress (ER stress, hypoxia, AA starvation).
Otherwise, it is activated when bound to GTP, and can help initiate translation of proteins.
**high levels of eiF2-P are assc with Alzheimers, Parkinson’s, Huntington’s indicating an increase in unfolded/misfolded proteins in the cells (ER stress)
eiF4E
normally inhibited by hypophosphorylated 4E-BP
insulin activates kinases that phosphorylate the 4E-BP, activating eiF4E and causing it to dissociate, increasing protein synthesis
mRNA binding proteins
regulate translation by dictating the 3D structure of the RNA thus blocking translation when bound to the mRNA.
Ex: iron response elements (IREs) in untranslated regions of mRNA and IRPs
iron response elements
IRPs bind iron when present, but otherwise bind the IREs, blocking translation at the 5’ end and stabilizing mRNA on the 3’ end
how do viruses hijack our machinery?
viruses use proteases to degrade our eiFs involved in cap-dependent translation, thus freeing up ribosomes for their own cap-independent use
they also use internal ribosome entry sites (IRES) which allow them to use ribosome without a cap on mRNA