The Role of Protein Synthesis and Degradation in the Post-Transcriptional Regulation of Rat Multidrug Resistance-Associated Protein 2 (Mrp2, Abcc2)

2005 ◽  
Vol 68 (3) ◽  
pp. 701-710 ◽  
Author(s):  
B. R. Jones ◽  
W. Li ◽  
J. Cao ◽  
T. A. Hoffman ◽  
P. M. Gerk ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Transcriptional Regulation ◽  
Multidrug Resistance ◽  
Post Transcriptional Regulation ◽  
Protein Synthesis And Degradation ◽  
Synthesis And Degradation

scholarly journals Abundance of hepatic metallothionein mRNA is increased by protein-synthesis inhibitors. Evidence for transcriptional activation and post-transcriptional regulation

1991 ◽  
Vol 273 (1) ◽  
pp. 185-188 ◽  
Author(s):  
C C McCormick ◽  
L M Salati ◽  
A G Goodridge
Keyword(s):  
Gene Expression ◽  
Protein Synthesis ◽  
Transcriptional Regulation ◽  
Transcriptional Activation ◽  
Actinomycin D ◽  
Protein Synthesis Inhibitors ◽  
Mrna Accumulation ◽  
Hepatic Metallothionein ◽  
Post Transcriptional Regulation

Ongoing protein synthesis is a prerequisite in the expression of some genes. We studied the effect of various protein synthesis inhibitors on the expression of the avian metallothionein (MT) gene. Chicken embryonic hepatocytes in culture were exposed to various concentrations of cycloheximide, puromycin and pactamycin. At concentrations which decreased total protein synthesis by about 90% each inhibitor increased MT mRNA accumulation approx. 5-fold at 9 h of incubation. Incubation with puromycin or zinc for 2 h markedly increased the rate of MT gene transcription. Estimates of the half-life of MT mRNA by using actinomycin D suggested for cycloheximide, but not puromycin, decreased the decay rate of MT mRNA. These data suggest the potential for post-transcriptional regulation of the avian MT gene. We conclude that different antibiotics increase the accumulation of hepatocyte MT mRNA by different mechanisms and that the possibility of multiple mechanisms should be considered in other studies of the role of protein synthesis in gene expression.

The role of nutrition in stimulating muscle protein accretion at the molecular level

2007 ◽  
Vol 35 (5) ◽  
pp. 1298-1301 ◽  
Author(s):  
S.R. Kimball
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Muscle Protein ◽  
Mrna Translation ◽  
Regulatory Proteins ◽  
Downstream Effectors ◽  
Regulate Protein ◽  
Protein Synthesis And Degradation ◽  
Synthesis And Degradation

Nutrients act both directly and indirectly to modulate muscle protein accretion through changes in protein synthesis and degradation. For example, glucose, amino acids and fatty acids can all be metabolized to produce energy in the form of ATP that can be utilized for protein synthesis. In addition, amino acids are used directly for the synthesis of new proteins. Nutrients also regulate protein synthesis through activation of a signalling pathway involving the protein kinase, mTOR [mammalian TOR (target of rapamycin)]. Together with several regulatory proteins, mTOR forms a complex referred to as TORC1 (TOR complex 1). Because of its central role in controlling cell growth, TORC1 is an integral component of the mechanism through which nutrients modulate protein synthesis. Herein, the mechanism(s) through which nutrients, and in particular amino acids, regulate signalling through TORC1 will be discussed. In addition, downstream effectors of TORC1 action on mRNA translation will be briefly presented. Finally, a previously unrecognized effector of TORC1 signalling in regulating protein synthesis will be described.

scholarly journals Fast and Efficient 5′P Degradome Library Preparation for Analysis of Co-Translational Decay in Arabidopsis

Plants ◽  
2021 ◽  
Vol 10 (3) ◽  
pp. 466
Author(s):  
Marie-Christine Carpentier ◽  
Cécile Bousquet-Antonelli ◽  
Rémy Merret
Keyword(s):  
Gene Expression ◽  
Quality Control ◽  
Transcriptional Regulation ◽  
High Throughput ◽  
Library Preparation ◽  
Working Day ◽  
Set Up ◽  
Post Transcriptional Regulation ◽  
Commercial Kit

The recent development of high-throughput technologies based on RNA sequencing has allowed a better description of the role of post-transcriptional regulation in gene expression. In particular, the development of degradome approaches based on the capture of 5′monophosphate decay intermediates allows the discovery of a new decay pathway called co-translational mRNA decay. Thanks to these approaches, ribosome dynamics could now be revealed by analysis of 5′P reads accumulation. However, library preparation could be difficult to set-up for non-specialists. Here, we present a fast and efficient 5′P degradome library preparation for Arabidopsis samples. Our protocol was designed without commercial kit and gel purification and can be easily done in one working day. We demonstrated the robustness and the reproducibility of our protocol. Finally, we present the bioinformatic reads-outs necessary to assess library quality control.

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