Prosomes discriminate between mRNA of adenovirus‐infected and uninfected HeLa cells

Horsch, Andrea; de, Cezar Martins; Dineva, Bistra; Spindler, Ernst; Schmid, Hans‐Peter

doi:10.1016/0014-5793(89)80268-6

Cited by 44 publications

(18 citation statements)

References 20 publications

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“…4); (ii) Arrigo et al (35) have demonstrated by RNA sequencing that Drosophila proteasomes are associated with RNA fragments that possess extended adenosine-and uridinerich elements; and (iii) finally, our RNase protection experiments confirmed that proteasomes interact specifically with the 3Ј end of a nondefined number of cytoplasmic RNAs. However, the binding site is not the poly(A) ϩ sequence because proteasome-associated RNA fragments reported so far do not have oligo(A) stretches, and proteasomes associate strongly with TMV-RNA without poly(A) ϩ or with adenovirus mRNAs of which the poly(A) ϩ tail is blocked by oligo(dT) (36). We suspect that proteasomes bind to sequences adjacent or within adenosine-and uridine-rich elements close to poly(A) ϩ and cleave the 3Ј end with the poly(A) ϩ sequences of the corresponding messengers.…”

Section: Discussionmentioning

confidence: 99%

Possible Involvement of Proteasomes (Prosomes) in AUUUA-mediated mRNA Decay

Jarrousse¹,

Petit²,

Kreutzer-Schmid³

et al. 1999

Journal of Biological Chemistry

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We have identified a cellular target for proteasomal endonuclease activity. Thus, 20 S proteasomes interact with the 3-untranslated region of certain cytoplasmic mRNAs in vivo, and 20 S proteasomes isolated from Friend leukemia virus-infected mouse spleen cells were found to be associated with a mRNA fragment showing great homology to the 3-untranslated region of tumor necrosis factor-␤ mRNA that contains AUUUA sequences. We furthermore demonstrate that 20 S proteasomes destabilize oligoribonucleotides corresponding to the 3-untranslated region of tumor necrosis factor-␣, creating a specific cleavage pattern. The cleavage reaction is accelerated with increasing number of AUUUA motifs, and major cleavage sites are localized at the 5 side of the A residues. These results strongly suggest that 20 S proteasomes could be involved in the destabilization of cytokine mRNAs such as tumor necrosis factor mRNAs and other short-lived mRNAs containing AUUUA sequences.

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Section: Discussionmentioning

confidence: 99%

Possible Involvement of Proteasomes (Prosomes) in AUUUA-mediated mRNA Decay

Jarrousse¹,

Petit²,

Kreutzer-Schmid³

et al. 1999

Journal of Biological Chemistry

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“…While no inhibition was observed with globin mRNA and cellular mRNAs of HeLa cells, the translation of TMV-RNA and mRNA isolated from adenovirusinfected HeLa cells was impeded (Horsch et al, 1989). Recent work of our laboratory indicates that proteasome prevents the formation of 80 S initiation complexes but not the early phase of initiation (Homma et al 1994).…”

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confidence: 90%

“…We and others have demonstrated that proteasomes can interfere with protein synthesis in vitro (Horsch et al, 1989;Lühn et al, 1990). While no inhibition was observed with globin mRNA and cellular mRNAs of HeLa cells, the translation of TMV-RNA and mRNA isolated from adenovirusinfected HeLa cells was impeded (Horsch et al, 1989).…”

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confidence: 99%

Identification and Initial Characterization of a Specific Proteasome (Prosome) Associated RNase Activity

Pouch

Petit

Buri

et al. 1995

Journal of Biological Chemistry

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We have identified and characterized a specific nuclease activity to be tightly associated with proteasomes. Using tobacco mosaic virus RNA (TMV-RNA) as substrate to analyze and quantify the cleavage reaction, we supply several lines of evidence that this nuclease activity is an integral part of proteasomes. Thus, RNase activity was coincident with the elution profiles of proteasomes at each stage of purification. Proteasomal nuclease activity was resistant to strong dissociation conditions using 480 mM KC1, 0.5% sodium lauroylsarcosinate, and 6 M urea. This nuclease activity remained associated with an urea-resistant subcomplex of the proteasome comprising a specific set of proteins. Finally the digestion of TMV-RNA led to a well defined pattern of RNA fragments while 5 S ribosomal RNA and globin mRNA were not degraded. These results provide further evidence that proteasomes are able to discriminate between different RNAs, and the possible involvement of proteasomes in translation control is discussed.

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“…Among the 'split factors' are the prosomes, a specific type of RNP of M , 720000, composed of variable sets of small proteins and RNA species that was discovered and characterized over the last years (Schmid et al, 1984;review in Scherrer, 1990). These particles, which have multi-catalytic proteinase activity (Rivett, 1989;Orlowski, 1990), might be involved in mRNA transport and differential pre-translational controls, being split off the mRNA in vivo prior to translation (Grainger and Winkler, 1987) and inhibit initiation of translation in vitro (Kleinschmidt and Buhl, 1987;Horsch et al, 1989). …”

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The protein of M_r 21 000 constituting the prosome‐like particle of duck erythroblasts is homologous to apoferritin

Coux

Camoin

Nothwang

et al. 1992

European Journal of Biochemistry

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In duck erythroblasts, two major populations of untranslated messenger (m) RNP can be separated by sucrose gradient centrifugation in low ionic strength. One of these contains globin mRNA associated to protein factors, among them the prosomes. The other, sedimenting in the 35S zone, contains non‐globin mRNA. From this ‘35S’ mRNP, a new RNP particle called the prosome‐like particle was isolated and characterized [Akhayat, O., Infante, A. A., Infante, D., Martins de Sa, C., Grossi de Sa, M.‐F. & Scherrer, K. (1987) Eur. J. Biochem. 170, 23–33]. The PLP is a multimer of a protein of Mr 21000, and contains small RNA species. The particle is tightly associated with repressed mRNA and inhibits in vitro protein synthesis. We show here that the protein of Mr 21000, constituting the prosome‐like particle, is apoferritin. Different approaches confirm the RNP character of this particle and provide evidence that some of its RNA species are tRNA. The hypothesis is discussed as to whether (apo–)ferritin might serve other functions in addition to iron storage.

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Prosomes discriminate between mRNA of adenovirus‐infected and uninfected HeLa cells

Cited by 44 publications

References 20 publications

Possible Involvement of Proteasomes (Prosomes) in AUUUA-mediated mRNA Decay

Possible Involvement of Proteasomes (Prosomes) in AUUUA-mediated mRNA Decay

Identification and Initial Characterization of a Specific Proteasome (Prosome) Associated RNase Activity

The protein of M_r 21 000 constituting the prosome‐like particle of duck erythroblasts is homologous to apoferritin

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Prosomes discriminate between mRNA of adenovirus‐infected and uninfected HeLa cells

Cited by 44 publications

References 20 publications

Possible Involvement of Proteasomes (Prosomes) in AUUUA-mediated mRNA Decay

Possible Involvement of Proteasomes (Prosomes) in AUUUA-mediated mRNA Decay

Identification and Initial Characterization of a Specific Proteasome (Prosome) Associated RNase Activity

The protein of Mr 21 000 constituting the prosome‐like particle of duck erythroblasts is homologous to apoferritin

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The protein of M_r 21 000 constituting the prosome‐like particle of duck erythroblasts is homologous to apoferritin