IV. Interactions with eRF3
Interactions between eRF1 and eRF3
occur in domain 3 of the protein from residues
. An intact domain 3 is crucial for this
, one of the central beta strands, is responsible for stabilizing the
domain. As a result, beta-15 is critical for
the interaction between eRF1 and eRF32.
In yeast, another key binding site for eRF3
occurs on the extreme C terminus of the
protein. However, the residues comprising the
C terminus of eRF1 in human eRF1 are
disordered and as such the C terminus has been
demonstrated to be unnecessary for human eRF1
and eRF3 interactions2.
1. Bertram G, Bell HA,
Ritchie DW, Fullerton G, Stansfield I. 2000.
Terminating eukaryote translation: Domain 1 of
release factor eRF1 functions in stop codon
recognition. RNA. 6:1236-1247.
2. Song H, Mugnier P,
Das AK, Webb HM, Evans DR, Tuite MF,
Hemmings BA, Barford D. 2000. The crystal
structure of human eukaryotic release factor
eRF1--Mechanism of stop codon recognition
and peptidyl-tRNA hydrolysis. Cell. 100:311-321.
3. Matheisl S,
Berninghausen O, Becker T, Beckmann R. 2015.
Structure of a human translation termination
complex. Nucleic Acids Res. 43:
4. Dubovaya VI, Kolosov
PM, Alkalaeva EZ, Yu L, Frolova, Kisselev
LL. 2006. Influence of individual domains of
the translation termination factor eRF1 on
induction of GTPase activity of the
translation termination factor eRF3. Molecular
5. Kisselev L. 2002.
Polypeptide release factors in prokaryotes
and eukaryotes: same function, different
structure. Structure. 10:8-9.
6. Nakamura Y, Ito K,
Ehrenberg M. 2000. Mimicry grasps reality in
translation termination. Cell.
7. Frolova L, Seit-Nebi
A, Kisselev L. 2002. Highly conserved NIKS
tetrapeptide is functionally essential in
eukaryotic translation termination factor
eRF1. RNA. 8:129-136.
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