Ribonucleotide sequences non-adjacent to poly(A) participate in the poly(A)-protein complex in 15S duck globin mRNP particles

Goldenberg, Samuel; Víncent, Alaín; Scherrer, Klaus

doi:10.1093/nar/8.21.5057

Cited by 15 publications

(4 citation statements)

References 36 publications

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“…In vitro, using purified PAN and PABP1, it has been shown that PAN-dependent deadenylylation can be regulated by sequences present in the 3Ј untranslated region (UTR) of mRNAs (42). Since PABP1 is also able to interact with some 3Ј-UTR sequences (43), it could participate in the control of the rate of deadenylylation and eventually deadenylylation-dependent decapping, as well as in determining the threshold length at which deadenylylation triggers decapping (39,40,42). While considering the hypothesis that PABP1 is involved in the control of the threshold poly(A) length that triggers decapping in mammalian cells, it should be noted that the upper limit of this threshold length for SAA mRNA (60 residues) should be sufficient to allow for binding of two PABP1 molecules (44).…”

Section: Traces Of Decapped Species With a Short Poly(a) Tail Can Be mentioning

confidence: 99%

Messenger RNA deadenylylation precedes decapping in mammalian cells

Couttet

Fromont‐Racine

Steel

et al. 1997

Proc. Natl. Acad. Sci. U.S.A.

197

191

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In yeast, the major mRNA degradation pathway is initiated by poly(A) tail shortening that triggers mRNA decapping. The mRNA is then degraded by 5-to-3 exonucleolysis. In mammalian cells, even though poly(A) tail shortening also precedes mRNA degradation, the degradation pathway has not been elucidated. We have used a reverse transcription-PCR approach that relies on mRNA circularization to measure the poly(A) tail length of four mammalian mRNAs. This approach allows for the simultaneous analysis of the 5 and 3 ends of the same mRNA molecule. For all four mRNAs analyzed, this strategy permitted us to demonstrate the existence of small amounts of decapped mRNA species which have a shorter poly(A) tail than their capped counterparts. Kinetic analysis of one of these mRNAs indicates that the decapped species with a short poly(A) tail are mRNA degradation products. Therefore, our results indicate that decapping is preceded by a shortening of the poly(A) tail in mammalian cells, as it is in yeast, suggesting that this mRNA degradation pathway is conserved throughout eukaryotic evolution.Messenger RNA degradation contributes significantly to the regulation of gene expression. In eukaryotes, elucidation of a number of mRNA degradation pathways is under way (for reviews, see refs 1-4). Presently, these pathways are better understood in yeast than in mammalian cells. Both in yeast and in mammalian cells, degradation of most polyadenylylated mRNAs appears to be initiated by poly(A) shortening: transcriptional pulse-chase experiments have shown that shortening of the poly(A) tail precedes mRNA degradation (5, 6). Some regulatory sequence determinants affect mRNA stability by modulating the rate of deadenylylation, whereas others modulate a later degradation step (5-7). This later step has been elucidated in yeast: deadenylylation at the 3Ј end triggers mRNA decapping at the 5Ј end, which is then followed by 5Ј-to-3Ј exonucleolysis (refs. 8 and 9 and references therein). In some specific circumstances, other degradation pathways are observed: exonucleolysis from the 3Ј end can occur when the 5Ј-to-3Ј exonuclease is inactive, and a decapping pathway independent of poly(A) tail shortening is involved in the degradation of mRNAs that show premature translation termination (9-11).In mammalian cells, the degradation pathway that follows deadenylylation is not well understood. Uncapped mRNAs are less stable than their capped counterparts in cell extracts, and enzymatic activities that catalyze mRNA decapping and 5Ј-to-3Ј exonucleolysis have been identified (refs. 1 and 3 and references therein). Furthermore, there is a conservation between yeast and mammalian cells of a functional interaction between the 5Ј and 3Ј ends of mRNAs: in both systems, these two ends contribute to translational control (e.g., see refs. 12 and 13). It is thus tempting to speculate that deadenylylation triggers a decapping-dependent degradation pathway in mammalian cells as well. However, a direct demonstration is lacking.We have developed a revers...

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Section: Traces Of Decapped Species With a Short Poly(a) Tail Can Be mentioning

confidence: 99%

Messenger RNA deadenylylation precedes decapping in mammalian cells

Couttet

Fromont‐Racine

Steel

et al. 1997

Proc. Natl. Acad. Sci. U.S.A.

197

191

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“…Comparison of duck mRNP proteins with those of mouse and rabbit mRNP ( fig.1 (1,6)) shows that the major protein component from the 3 species displays the same Mr-value. In order to see whether, as in the case of duck polyribosomal mRNP, this protein was associated with the poly(A) fragment [6,8], duck and mouse polyribosomes were treated with ribonucleases A and Tx and the proteins recovered in the poly(A)-RNP particles were compared (riga (3,4)). In both cases the 73 000 M r protein is the major protein which binds to poly(A).…”

Section: Resultsmentioning

confidence: 99%

The polyribosomal poly(A)‐binding protein is highly conserved in vertebrate species

1981

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“…This could be due to the presence of certain proteins, notably a protein or proteins of approximately 78000 molecular weight, which are known to be localised on the poly(A) tail of numerous polyribosomal mRNA species (reviewed in [19][20][21] and partially protect the poly(A) tail against digestion by nuclease (22). It has been shown that poly(A) rich RNA-protein complexes recovered after RNAase digestion of mRNP contain some additional nucleotide sequences other than poly(A) (23)(24)(25), [32PImRNA was translated in a messenger dependent cell free system and the lysates were fractionated as described for Fig. 4: (a) uninhibited lysate; (b) and (c) lysate inhibited by 10 mM NaF.…”

Section: Discussionmentioning

confidence: 99%

“…Thus the terminus of the 3'poly(A) tail may be less accessible due to protection of terminal sequences or possibly by stabilisation of certain secondary structures involving the poly(A) tail by ribonucleoproteins. In view of reports that the polyribosomal mRNP complex is a dynamic structure (25,27) and that sequences from the 5'-end non-coding region may interact with sequences from the 3'-end (28), visualised as circular mRNAs in electron micrographs (29), it would now be very interesting to probe for the accessibility of the poly(A) tail to labelling with T4 RNA ligase in initiation complexes and in various polysome size classes.…”

Section: Discussionmentioning

confidence: 99%

An alternative management system for Alaska Reindeer Herds

Thomas

Arobio

Naylor

et al. 1983

Agricultural Systems

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Rabbit polyribosomal globin messenger RNA (mRNA) and messenger ribonucleoprotein (mRNP) were labelled at the 3' poly(A) tail to high specific activity with T4 RNA ligase and [5'-(32)P]pCp without consequent loss of functional activity. Labelled message was translated in both micrococcal nuclease treated and untreated rabbit reticulocyte lysates, as shown by the formation of labelled polyribosomes. The utilisation of labelled messenger was abolished by T2 toxin or sodium fluoride which are known to inhibit protein synthesis.Images

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Ribonucleotide sequences non-adjacent to poly(A) participate in the poly(A)-protein complex in 15S duck globin mRNP particles

Cited by 15 publications

References 36 publications

Messenger RNA deadenylylation precedes decapping in mammalian cells

Messenger RNA deadenylylation precedes decapping in mammalian cells

The polyribosomal poly(A)‐binding protein is highly conserved in vertebrate species

An alternative management system for Alaska Reindeer Herds

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