Mouse GSPT2, but not GSPT1, can substitute for yeast eRF3 in vivo

C.L. Goff, O. Zemlyanko, S. Moskalenko, N. Berkova, S. Inge-Vechtomov, M. Philippe, G. Zhouravleva

Результат исследований: Научные публикации в периодических изданияхстатья

23 Цитирования (Scopus)

Выдержка

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
Язык оригиналаанглийский
Страницы (с-по)1043-1057
ЖурналGenes to Cells
Номер выпуска10
СостояниеОпубликовано - 2002
Опубликовано для внешнего пользованияДа

Отпечаток

Yeasts
Essential Genes
Eukaryota
Genes
Mammals
Proteins
Amino Acids
Peptides
Mutation

Цитировать

@article{68467e527bc141bab3ca6a36ca2e2e89,
title = "Mouse GSPT2, but not GSPT1, can substitute for yeast eRF3 in vivo",
abstract = "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",
author = "C.L. Goff and O. Zemlyanko and S. Moskalenko and N. Berkova and S. Inge-Vechtomov and M. Philippe and G. Zhouravleva",
year = "2002",
language = "English",
pages = "1043--1057",
journal = "Genes to Cells",
issn = "1356-9597",
publisher = "Wiley-Blackwell",
number = "10",

}

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.

В: Genes to Cells, № 10, 2002, стр. 1043-1057.

Результат исследований: Научные публикации в периодических изданияхстатья

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 -