elongation factor 1β
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2001 ◽  
Vol 1527 (3) ◽  
pp. 130-140 ◽  
Author(s):  
Ruth Furukawa ◽  
Tim M Jinks ◽  
Tomer Tishgarten ◽  
Mark Mazzawi ◽  
Donald R Morris ◽  
...  

1999 ◽  
Vol 19 (8) ◽  
pp. 5257-5266 ◽  
Author(s):  
Anne Carr-Schmid ◽  
Louis Valente ◽  
Valerie I. Loik ◽  
Tanishia Williams ◽  
Lea M. Starita ◽  
...  

ABSTRACT Translation elongation factor 1β (EF-1β) is a member of the family of guanine nucleotide exchange factors, proteins whose activities are important for the regulation of G proteins critical to many cellular processes. EF-1β is a highly conserved protein that catalyzes the exchange of bound GDP for GTP on EF-1α, a required step to ensure continued protein synthesis. In this work, we demonstrate that the highly conserved C-terminal region of Saccharomyces cerevisiae EF-1β is sufficient for normal cell growth. This region of yeast and metazoan EF-1β and the metazoan EF-1β-like protein EF-1δ is highly conserved. Human EF-1β, but not human EF-1δ, is functional in place of yeast EF-1β, even though both EF-1β and EF-1δ have previously been shown to have guanine nucleotide exchange activity in vitro. Based on the sequence and functional homology, mutagenesis of two C-terminal residues identical in all EF-1β protein sequences was performed, resulting in mutants with growth defects and sensitivity to translation inhibitors. These mutants also enhance translational fidelity at nonsense codons, which correlates with a reduction in total protein synthesis. These results indicate the critical function of EF-1β in regulating EF-1α activity, cell growth, translation rates, and translational fidelity.


1999 ◽  
Vol 63 (4) ◽  
pp. 666-671 ◽  
Author(s):  
Katsuyoshi KAMIIE ◽  
Hideharu TAIRA ◽  
Kohmei KOBAYASHI ◽  
Tetsuro YAMASHITA ◽  
Shin-ichiro KIDOU ◽  
...  

1998 ◽  
Vol 12 (1) ◽  
pp. 1-6 ◽  
Author(s):  
Giuseppe Ianniciello ◽  
Mariorosario Masullo ◽  
Gennaro Raimo ◽  
Paolo Arcari ◽  
Vincenzo Bocchini

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