Chapter 12: Regulation of Translation Flashcards
Translation rates respond to the () of the cell, reflected in the amount of amino acids present
nutritional state
In bacteria, () compete with charged tRNAs for binding at the A site
uncharged tRNAs
binding of uncharged tRNA in A site of bacterial ribosome results in recruitment of ()
RelA
RelA synthesizes lots of (p)ppGpp (a pentaphosphate guanine nucleotide called “()”) from GTP/GDP and ATP precursors.
magic spot
action of RelA modulates transcription and induces stress responses to replenish amino acids. This is called the “()”
stringent response
In eukaryotes, the uncharged tRNA binds to ();
Gcn2
When bound to tRNA, a kinase domain in Gcn2 phosphorylates the initiation factor () in euks.
eIF2
Phosphorylated eIF2 binds strongly to () (to the point where active eIF2 is effectively depleted from the cell), and cannot then be used for initiation, so translation is shut dow
eIF2B
Normally, eIF2 binds to eIF2B and exchanges ()
GDP for GTP
Phosphorylation at () results in constitutive binding of eIF2 to eIF2B, inhibiting translation initiation
serine 51 of the eIF2 alpha subunit
mRNAs compete for ()–this is another opportunity for translational regulation
translation machinery
eIF4E can be sequestered by a range of () in response to cellular conditions- this decreases overall translation activity
4E-BPs (eIF4E – Binding Proteins)
mRNAs assume () in different conditions–and these affect translation levels
different shapes
In bacteria,the Shine-Dalgarno sequence is often (), preventing translation initiation
obscured
() are another example-these small regulatory molecules control their own synthesis
Riboswitches
one riboswitch example is ()
thiamine synthesis
Another example of regulated SD sequestration mediated by protein: control of the expression of () in E.coli
threonine tRNA synthetase