Inactive mRNA-protein complexes from mouse sarcoma-180 ascites cells.

Geoghegan, Thomas; Cereghini, Silvia; Brawerman, George

doi:10.1073/pnas.76.11.5587

Cited by 46 publications

(41 citation statements)

References 22 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Nuclei and cell debris were removed by centrifugation at 1,000 x g for 10 min and washed with 1 volume of 1 x lysing buffer. The combined supernatants were fractionated by zone centrifugation, and RNA was isolated from pooled fractions by phenol extraction as described previously (9 (8).…”

Section: Methodsmentioning

confidence: 99%

“…The high levels of P40 and P36 mRNAs in the RNP fractions are not a true reflection of their distribution between the active and untranslated compartments, since the total mRNF , respectively, were translated in the wheat germ cell-free system. The sarcoma preparations were obtained as described previously (8). Translation products other than actin are designated by their approximate molecular weights.…”

Section: Methodsmentioning

confidence: 99%

“…A substantial portion of the cellular mRNA is usually present as small particles not associated with ribosomes. The untranslated fraction of several types of cells has been shown to be enriched in a limited population of mRNA species (5,8,14). Some relatively abundant mRNA species have been identified in the untranslated fraction of mouse sarcoma-180 ascites cells (8).…”

mentioning

confidence: 99%

“…The untranslated fraction of several types of cells has been shown to be enriched in a limited population of mRNA species (5,8,14). Some relatively abundant mRNA species have been identified in the untranslated fraction of mouse sarcoma-180 ascites cells (8). They represent functional molecules apparently maintained in an inactive state through interaction with protein components (2).…”

mentioning

confidence: 99%

See 3 more Smart Citations

Regulation of mRNA utilization in mouse erythroleukemia cells induced to differentiate by exposure to dimethyl sulfoxide.

Yenofsky¹,

Cereghini²,

Krowczynska³

et al. 1983

Mol. Cell. Biol.

Self Cite

123

View full text Add to dashboard Cite

Mouse erythroleukemia cells contain several abundant mRNA species that occur to a considerable extent as untranslated molecules. For two of these species, which code for polypeptides P40 and P21, the proportion of molecules engaged in translation decreases rapidly after exposure of the cells to dimethyl sulfoxide. The extent of utilization of a third species, the P36 mRNA, is not altered. The rate of production of the P40 mRNA does not appear to be affected in the dimethyl sulfoxide-treated cells. The P21 mRNA appears to be produced in increasing amounts, leading to a large accumulation of untranslated molecules in the cytoplasm. The mRNA for actin remains nearly fully utilized during this process, but its intracellular concentration decreases, thus resulting in a reduction in the amounts present in polysomes. The results indicate that some mRNA species in mouse tumor cells are subject to a translational repression process that can serve to regulate selectively the extent of expression of the corresponding genes.

show abstract

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

See 2 more Smart Citations

Regulation of mRNA utilization in mouse erythroleukemia cells induced to differentiate by exposure to dimethyl sulfoxide.

Yenofsky¹,

Cereghini²,

Krowczynska³

et al. 1983

Mol. Cell. Biol.

Self Cite

123

View full text Add to dashboard Cite

show abstract

“…In cultured mammalian cells between 20 and 50% of cytoplasmic mRNA exists in untranslated mRNPs (6,11,24). There are a number of possibilities for the fate of this mRNA.…”

mentioning

confidence: 99%

Regulation of the utilization of mRNA for eucaryotic elongation factor Tu in Friend erythroleukemia cells.

Rao¹,

Slobin²

1987

Mol. Cell. Biol.

View full text Add to dashboard Cite

When Friend erythroleukemia cells were allowed to grow to stationary phase (2 X 10(6) to 3 X 10(6) cells per ml), approximately 60% of the mRNA for eucaryotic elongation factor Tu (eEF-Tu) sedimented at less than or equal to 80S, and most of the remaining factor mRNA was associated with small polysomes. Under the same growth conditions, greater than 90% of the mRNA for eucaryotic initiation factor 4A remained associated with polysomes. The association of eEF-Tu mRNA with polysomes changed dramatically when stationary-phase cells were treated with fresh medium. After 1 h in fresh medium, approximately 90% of eEF-Tu mRNA in Friend cells was found in heavy polysomes. Associated with the shift of eEF-Tu mRNA into heavy polysomes, we found at least a 2.6-fold increase in the synthesis of eEF-Tu in vivo as well as a remarkable 40% decrease in the total amount of eEF-Tu mRNA per cell. Our data raise the possibility that eEF-Tu mRNA that has accumulated in ribonucleoprotein particles in stationary-phase cells is degraded rather than reutilized for eEF-Tu synthesis.

show abstract

Differential repression of specific mRNA in erythroblast cytoplasm: a possible role for free mRNP proteins.

Víncent¹,

Akhayat²,

Goldenberg³

et al. 1983

The EMBO Journal

View full text Add to dashboard Cite

Two types of in vivo untranslated ‘free’ mRNA‐protein particles (mRNP) were isolated from duck erythroblast cytoplasm and characterised. Both types, namely the highly purified globin mRNA‐specific ‘20S’ mRNP and the ‘35S’ mRNP containing a heterogenous non‐globin mRNA population, are not translatable in rabbit reticulocyte lysates, but yield active mRNA upon deproteinisation. In vivo, 90% of globin mRNA is translated, but the majority of mRNA types are found in the inactive mRNP fraction, including fully repressed mRNA species. Searching for the factors controlling differential mRNA repression, we characterised and compared the protein composition of globin and ‘35S’ mRNP using two dimensional gel electrophoresis, in vivo labelling with [35S]methionine and in vivo phosphorylation. The major proteins ubiquitously bound to globin or any other mRNA in the polyribosomes (e.g., the 73 K mol. wt. poly(A) binding protein) were not detected in purified inactive mRNP. In the latter some polypeptides appear to be associated with only one of the two inactive mRNA types while some others are common to both mRNPs. Furthermore, different rates of synthesis and phosphorylation characterize the protein populations of the two types of repressed mRNP. The specificity in composition and metabolism of the populations of polypeptides associated with different subpopulations of inactive cytoplasmic mRNA, as shown here, argues in favour of a role of mRNP proteins in mRNA recognition and selective translational repression, possibly in association with the ScRNA previously found as components of the free mRNP and able to inhibit protein synthesis.

show abstract

Inactive mRNA-protein complexes from mouse sarcoma-180 ascites cells.

Cited by 46 publications

References 22 publications

Regulation of mRNA utilization in mouse erythroleukemia cells induced to differentiate by exposure to dimethyl sulfoxide.

Regulation of mRNA utilization in mouse erythroleukemia cells induced to differentiate by exposure to dimethyl sulfoxide.

Regulation of the utilization of mRNA for eucaryotic elongation factor Tu in Friend erythroleukemia cells.

Differential repression of specific mRNA in erythroblast cytoplasm: a possible role for free mRNP proteins.

Contact Info

Product

Resources

About