scholarly journals Identification of an mRNP Complex Regulating Tumorigenesis at the Translational Elongation Step

2011 ◽  
Vol 41 (4) ◽  
pp. 419-431 ◽  
Author(s):  
George S. Hussey ◽  
Arindam Chaudhury ◽  
Andrea E. Dawson ◽  
Daniel J. Lindner ◽  
Charlotte R. Knudsen ◽  
...  
Keyword(s):  
Mrnp Complex ◽  
Elongation Step

scholarly journals The Ras/PKA Signaling Pathway May Control RNA Polymerase II Elongation via the Spt4p/Spt5p Complex in Saccharomyces cerevisiae

Genetics ◽  
2003 ◽  
Vol 165 (3) ◽  
pp. 1059-1070
Author(s):  
Susie C Howard ◽  
Arelis Hester ◽  
Paul K Herman
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Growth ◽  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Signaling Pathway ◽  
Elongation Factor ◽  
Ras Signaling ◽  
Elongation Step ◽  
Rna Polymerase Ii Transcription

Abstract The Ras signaling pathway in Saccharomyces cerevisiae controls cell growth via the cAMP-dependent protein kinase, PKA. Recent work has indicated that these effects on growth are due, in part, to the regulation of activities associated with the C-terminal domain (CTD) of the largest subunit of RNA polymerase II. However, the precise target of these Ras effects has remained unknown. This study suggests that Ras/PKA activity regulates the elongation step of the RNA polymerase II transcription process. Several lines of evidence indicate that Spt5p in the Spt4p/Spt5p elongation factor is the likely target of this control. First, the growth of spt4 and spt5 mutants was found to be very sensitive to changes in Ras/PKA signaling activity. Second, mutants with elevated levels of Ras activity shared a number of specific phenotypes with spt5 mutants and vice versa. Finally, Spt5p was efficiently phosphorylated by PKA in vitro. Altogether, the data suggest that the Ras/PKA pathway might be directly targeting a component of the elongating polymerase complex and that this regulation is important for the normal control of yeast cell growth. These data point out the interesting possibility that signal transduction pathways might directly influence the elongation step of RNA polymerase II transcription.

Ribosomal protein eL42 contributes to the catalytic activity of the yeast ribosome at the elongation step of translation

Biochimie ◽  
2019 ◽  
Vol 158 ◽  
pp. 20-33 ◽  
Author(s):  
Codjo Hountondji ◽  
Jean-Bernard Créchet ◽  
Mayo Tanaka ◽  
Mieko Suzuki ◽  
Jun-ichi Nakayama ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Ribosomal Protein ◽  
Elongation Step

scholarly journals Human Immunodeficiency Virus Type 1 Vif Protein Is an Integral Component of an mRNP Complex of Viral RNA and Could Be Involved in the Viral RNA Folding and Packaging Process

2000 ◽  
Vol 74 (18) ◽  
pp. 8252-8261 ◽  
Author(s):  
Hui Zhang ◽  
Roger J. Pomerantz ◽  
Geethanjali Dornadula ◽  
Yong Sun
Keyword(s):  
Human Immunodeficiency Virus ◽  
Rna Binding ◽  
Viral Rna ◽  
Immunodeficiency Virus ◽  
Mrnp Complex ◽  
Rna Interaction ◽  
Vif Protein ◽  
Hiv 1

ABSTRACT Virion infectivity factor (Vif) is a protein encoded by human immunodeficiency virus types 1 and 2 (HIV-1 and -2) and simian immunodeficiency virus, plus other lentiviruses, and is essential for viral replication either in vivo or in culture for nonpermissive cells such as peripheral blood lymphoid cells, macrophages, and H9 T cells. Defects in the vif gene affect virion morphology and reverse transcription but not the expression of viral components. It has been shown that Vif colocalizes with Gag in cells and Vif binds to the NCp7 domain of Gag in vitro. However, it seems that Vif is not specifically packaged into virions. The molecular mechanism(s) for Vif remains unknown. In this report, we demonstrate that HIV-1 Vif is an RNA-binding protein and specifically binds to HIV-1 genomic RNA in vitro. Further, Vif binds to HIV-1 RNA in the cytoplasm of virus-producing cells to form a 40S mRNP complex. Coimmunoprecipitation and in vivo UV cross-linking assays indicated that Vif directly interact with HIV-1 RNA in the virus-producing cells. Vif-RNA binding could be displaced by Gag-RNA binding, suggesting that Vif protein in the mRNP complex may mediate viral RNA interaction with HIV-1 Gag precursors. Furthermore, we have demonstrated that these Vif mutants that lose the RNA binding activity in vitro do not supportvif-deficient HIV-1 replication in H9 T cells, suggesting that the RNA binding capacity of Vif is important for its function. Further studies regarding Vif-RNA interaction in virus-producing cells will be important for studying the function of Vif in the HIV-1 life cycle.

The Influence of the Glycerol-3-Phosphate Level in the Stroma Space on Lipid Synthesis of Intact Chloroplasts

1983 ◽  
Vol 38 (5-6) ◽  
pp. 399-404 ◽  
Author(s):  
Andreas Sauer ◽  
Klaus-Peter Heise
Keyword(s):  
Fatty Acid ◽  
Palmitic Acid ◽  
Silicone Oil ◽  
Lipid Synthesis ◽  
Fatty Acid Fraction ◽  
Chain Elongation ◽  
Acyl Acceptor ◽  
Chloroplast Stroma ◽  
Elongation Step ◽  
Coa Thioesters

The G3P level in chloroplasts, rapidly isolated from spinach leaves during a light-dark cycle, oscillated between 2.5 and 4 nmol · mg-1 Chi, which corresponds to a concentration of nearly 0.1 -0.2 mᴍ. In order to study the role of the stromal G3P level on chloroplast lipid biosynthesis, G3P uptake, measured by silicone oil centrifugation, has been correlated with the lipid synthesizing capacity of intact spinach chloroplasts. The level of G3P in the chloroplast stroma was decreased by high orthophosphate (Pi) concentrations in the medium. This decrease was caused by a strong Pi transport into the stroma, which is counterbalanced by a release of phosphorylated metabolites including G3P, mediated by the translocator. But because the reduced stromal G3P concentration exceeded about 3 times that for half saturation of the primary G3P acylation with oleoyl-ACP as preferred fatty acid donor, glycerolipid synthesis was not eliminated. Instead, the lowered G3P level in the stroma space limited the secondary acyla­tion step, indicated by the reduced incorporation of palmitic acid into the diglyceride fraction, and led to an accumulation of free oleic acid. Thus, beside its function as primary acyl acceptor, the stromal G3P level apparently controls the pool size of ACP bound palmitic acid by limitation of the chain elongation step from palmitoyl- to stearoyl-ACP in order to induce the specific palmitic acid channeling into the C-2-position of chloroplast lipids by the secondary G3P acylation. A similar function may be due to fatty acid consuming reactions from outside the chloroplast like acyl-CoA thioester formation in the outer envelope membrane, stimulated by exogenous CoA and ATP. In contradiction to earlier findings intact Percoll chloroplasts showed a measurable glycerolipid labelling (3-4%) from exogenous [14C]oleoyl-CoA in the presence of G3P (0.5 mᴍ), although most of the radioactivity was found in the free fatty acid fraction (7-10%). Incorporation into diglycerides was increased two-fold under fatty acid synthesizing conditions in the medium and the resulting diglycerides were further galactosylated by UDP- galactose addition. The latter observations suggest, that even in spite of the envelope imperme­ability for physiological concentrations of long-chain acyl-CoA thioesters, fatty acid transfer from these substrates to typical chloroplast lipids cannot be totally excluded.

scholarly journals Mechanism of action of purpuromycin

1992 ◽  
Vol 284 (1) ◽  
pp. 47-52 ◽  
Author(s):  
P Landini ◽  
E Corti ◽  
B P Goldstein ◽  
M Denaro
Keyword(s):  
Protein Synthesis ◽  
Rna Synthesis ◽  
Intact Cell ◽  
Acid Synthesis ◽  
Free System ◽  
Dna And Rna ◽  
Dna And Rna Synthesis ◽  
Dependent Protein ◽  
Elongation Step

Purpuromycin, an antibiotic active against both fungi and bacteria, shows different modes of action against these two kinds of micro-organisms; in Candida albicans it inhibits RNA synthesis, whereas in Bacillus subtilis protein synthesis is primarily affected, with DNA and RNA synthesis blocked at higher concentrations of the drug. In bacterial cell-free protein-synthesis systems, purpuromycin did not inhibit synthesis from endogenous mRNA (elongation of peptides initiated within the intact cell) but inhibited MS2-phase RNA-dependent protein synthesis (which requires initiation) by 50% at 0.1 mg/l. Poly(U)-directed polyphenylalanine synthesis was 50% inhibited by 20 mg of purpuromycin/l when added to a complete system; however, when purpuromycin was preincubated with ribosomes dissociated into 30 S and 50 S subunits, the concentration for 50% inhibition fell to 0.1 mg/l. By contrast, in a C. albicans cell-free system poly(U)-directed polyphenylalanine synthesis was partially inhibited only at 200 mg/l. Purpuromycin also inhibited polynucleotide synthesis in vitro in reactions using Escherichia coli or wheat-germ RNA polymerases or E. coli DNA polymerase I. We suggest that in bacteria the primary target of purpuromycin is on ribosomes and that its action precedes the elongation step of protein synthesis. The effect on nucleic acid synthesis in both fungi and bacteria may be due to interaction of purpuromycin with DNA.

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