Normal Cellular Protein Synthesis and Heat Shock

1994 ◽  
pp. 61-76 ◽  
Author(s):  
Mark R. Brodl ◽  
Jacqueline D. Campbell ◽  
Kent K. Grindstaff ◽  
Lora Fielding
Keyword(s):  
Protein Synthesis ◽  
Heat Shock ◽  
Cellular Protein ◽  
Cellular Protein Synthesis

Le transport de la phénylalanine et de la tyrosine chez Brevibacterium linens : spécificité et incorporation dans les protéines

1984 ◽  
Vol 30 (4) ◽  
pp. 430-438 ◽  
Author(s):  
P. Boyaval ◽  
Evelyne Moreira ◽  
M. J. Desmazeaud
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Cellular Protein ◽  
Cellular Proteins ◽  
Resting Cells ◽  
Brevibacterium Linens ◽  
Competitive Inhibitors ◽  
High Concentrations ◽  
Cellular Protein Synthesis

The specificity of phenylalanine and tyrosine carriers was investigated using actively metabolizing cells of Brevibacterium linens. The cellular protein synthesis of resting cells was very weakly inhibited, even with high concentrations of chloramphenicol or tetracycline. The nonaromatic amino acids were weak inhibitors for these carriers, while fluorinated analogues of phenylalanine and tyrosine were very potent competitive inhibitors. In practice these analogues cannot be used to replace amino acids to evaluate transport without incorporation because they are incorporated in cellular proteins.

Adenovirus E1A requires synthesis of a cellular protein to establish a stable transcription complex in injected Xenopus laevis oocytes

1987 ◽  
Vol 7 (9) ◽  
pp. 3049-3056
Author(s):  
J D Richter ◽  
H C Hurst ◽  
N C Jones
Keyword(s):  
Protein Synthesis ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Protein 70 ◽  
Mammalian Cells ◽  
Cellular Protein ◽  
Xenopus Laevis Oocytes ◽  
Protein Synthesis Inhibitors ◽  
Adenovirus E1a ◽  
High Level

The Escherichia coli-expressed adenovirus E1A 13S mRNA product injected into Xenopus oocytes was active, as assessed by its ability to stimulate the transcription of an injected gene which is normally responsive to E1A in mammalian cells. In the presence of the protein synthesis inhibitors pactamycin or cycloheximide, E1A was correctly posttranslationally modified (phosphorylated) and transported to the nucleus; but it failed to stimulate the transcription of an injected gene containing the human heat shock protein 70 promoter. The basal (unstimulated) level of transcription of the gene was unaffected by these inhibitors. If oocytes were cultured in the presence of cycloheximide after E1A stimulated transcription, however, the high level of transcription was maintained for several hours without new protein synthesis. Results of competition studies with the same promoter (the heat shock protein 70 promoter) linked to two marked genes demonstrated that once the induction of transcription by E1A took place, the stimulated levels of transcription were maintained, even when they were challenged with excess competitor DNA. Results of these studies suggest that E1A requires the synthesis of a cellular protein to form a stable transcription complex.

Effect of adenovirus on metabolism of specific host mRNAs: transport control and specific translational discrimination

1983 ◽  
Vol 3 (7) ◽  
pp. 1212-1221 ◽  
Author(s):  
A Babich ◽  
L T Feldman ◽  
J R Nevins ◽  
J E Darnell ◽  
C Weinberger
Keyword(s):  
Protein Synthesis ◽  
Host Cell ◽  
Cellular Protein ◽  
Host Protein ◽  
Cell Protein ◽  
Viral Mrna ◽  
Initiation Of Translation ◽  
Viral Mutant ◽  
Cellular Mrnas ◽  
Cellular Protein Synthesis

We have studied the adenovirus-induced inhibition of host cell protein synthesis and the effect of infection on the overall metabolism of host cell mRNA during the late phase of adenovirus infection by following the fate of a number of cellular mRNAs complementary to specific cloned DNA segments. At a time in infection when the rate of total cellular protein synthesis is drastically (greater than 90%) reduced, transcription of specific cellular genes is undiminished. However, the transport of newly synthesized cellular mRNA to the cytoplasm is greatly decreased. This decreased appearance of new mRNA in the cytoplasm cannot account for the observed cessation of cell specific protein synthesis, however, since the concentration of several preexisting cellular mRNAs, including the mRNA for actin, remains unchanged throughout the course of infection. The preexisting mRNA is intact, capped, and functional as judged by its ability to direct protein synthesis in vitro in a cap-dependent fashion. The interruption in host translation appears to operate at the level of initiation directly, since we find that fewer ribosomes are associated with a given cellular mRNA after infection than before infection. Furthermore, the in vivo inhibition of cellular protein synthesis does not appear to be the result of competition with viral mRNA, since conditions which prevent the efficient initiation of translation of viral mRNA (infection with a viral mutant) do not result in the recovery of cell translation. Thus, it appears that a late adenovirus gene product directly mediates a shutoff of host protein synthesis.

scholarly journals Structural Basis for Competitive Inhibition of eIF4G-Mnk1 Interaction by the Adenovirus 100-Kilodalton Protein

2004 ◽  
Vol 78 (14) ◽  
pp. 7707-7716 ◽  
Author(s):  
Rafael Cuesta ◽  
Qiaoran Xi ◽  
Robert J. Schneider
Keyword(s):  
Protein Synthesis ◽  
Competitive Inhibition ◽  
Late Phase ◽  
Mrna Translation ◽  
Cellular Protein ◽  
Structural Basis ◽  
Binding Motif ◽  
Amino Acid Peptide ◽  
Cellular Mrnas ◽  
Cellular Protein Synthesis

ABSTRACT Translation of most cellular mRNAs involves cap binding by the translation initiation complex. Among this complex of proteins are cap-binding protein eIF4E and the eIF4E kinase Mnk1. Cap-dependent mRNA translation generally correlates with Mnk1 phosphorylation of eIF4E when both are bound to eIF4G. During the late phase of adenovirus (Ad) infection translation of cellular mRNA is inhibited, which correlates with displacement of Mnk1 from eIF4G by the viral 100-kDa (100K) protein and dephosphorylation of eIF4E. Here we describe the molecular mechanism for 100K protein displacement of Mnk1 from eIF4G and elucidate a structural basis for eIF4G interaction with Mnk1 and 100K proteins and Ad inhibition of cellular protein synthesis. The eIF4G-binding site is located in an N-terminal 66-amino-acid peptide of 100K which is sufficient to bind eIF4G, displace Mnk1, block eIF4E phosphorylation, and inhibit eIF4F (cap)-dependent cellular mRNA translation. Ad 100K and Mnk1 proteins possess a common eIF4G-binding motif, but 100K protein binds more strongly to eIF4G than does Mnk1. Unlike Mnk1, for which binding to eIF4G is RNA dependent, competitive binding by 100K protein is RNA independent. These data support a model whereby 100K protein blocks cellular protein synthesis by coopting eIF4G and cap-initiation complexes regardless of their association with mRNA and displacing or blocking binding by Mnk1, which occurs only on preassembled complexes, resulting in dephosphorylation of eIF4E.

Pyridalyl inhibits cellular protein synthesis in insect, but not mammalian, cell lines

2008 ◽  
Vol 69 (1) ◽  
pp. 22-31 ◽  
Author(s):  
Koko Moriya ◽  
Setsuko Hirakura ◽  
Jun Kobayashi ◽  
Yoshihisa Ozoe ◽  
Shigeru Saito ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Cell Lines ◽  
Mammalian Cell ◽  
Cellular Protein ◽  
Mammalian Cell Lines ◽  
Cellular Protein Synthesis
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