Mouse GSPT2, but not GSPT1, can substitute for yeast eRF3 in vivo. / Goff, C.L.; Zemlyanko, O.; Moskalenko, S.; Berkova, N.; Inge-Vechtomov, S.; Philippe, M.; Zhouravleva, G.
In: Genes to Cells, No. 10, 2002, p. 1043-1057.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Mouse GSPT2, but not GSPT1, can substitute for yeast eRF3 in vivo
AU - Goff, C.L.
AU - Zemlyanko, O.
AU - Moskalenko, S.
AU - Berkova, N.
AU - Inge-Vechtomov, S.
AU - Philippe, M.
AU - Zhouravleva, G.
PY - 2002
Y1 - 2002
N2 - Background: The termination of protein synthesis in eukaryotes involves at least two polypeptide release factors (eRFs), eRF1 and eRF3. In mammals two genes encoding eRF3 structural homologues were identified and named GSPT1 and GSPT2. Results: In the present study, we demonstrate that mouse mGSPT2 but not mGSPT1 could functionally substitute the essential yeast gene SUP35. However, we show that the complementation property of mGSPT1 protein is modified when NH2-tagged by GST. Since mGSPT1 and mGSPT2 differ mainly in their N-terminal regions, we developed a series of N-terminal deleted constructs and tested them for complementation in yeast. We found that at least amino acids spanning 84-120 of mGSPT1 prevent the complementation of sup35 mutation.The fact that chimeras between mGSPT1, mGSPT2 and yeast Sup35 complement the disruption of the SUP35 gene indicates that the N-terminal region of mGSPT1 is not sufficient by itself to prevent complementation. Complementation of the mutant with a double disruption of
AB - Background: The termination of protein synthesis in eukaryotes involves at least two polypeptide release factors (eRFs), eRF1 and eRF3. In mammals two genes encoding eRF3 structural homologues were identified and named GSPT1 and GSPT2. Results: In the present study, we demonstrate that mouse mGSPT2 but not mGSPT1 could functionally substitute the essential yeast gene SUP35. However, we show that the complementation property of mGSPT1 protein is modified when NH2-tagged by GST. Since mGSPT1 and mGSPT2 differ mainly in their N-terminal regions, we developed a series of N-terminal deleted constructs and tested them for complementation in yeast. We found that at least amino acids spanning 84-120 of mGSPT1 prevent the complementation of sup35 mutation.The fact that chimeras between mGSPT1, mGSPT2 and yeast Sup35 complement the disruption of the SUP35 gene indicates that the N-terminal region of mGSPT1 is not sufficient by itself to prevent complementation. Complementation of the mutant with a double disruption of
M3 - Article
SP - 1043
EP - 1057
JO - Genes to Cells
JF - Genes to Cells
SN - 1356-9597
IS - 10
ER -
ID: 5008935