Mechanism and site of action of a ribosome‐inactivating protein type 1 from <i>Dianthus barbatus</i> which inactivates <i>Escherichia coli</i> ribosomes

Prestle, J.; Hornung, Ellen; Schönfelder, Max; Mundry, Karl-Wolfgang

doi:10.1016/0014-5793(92)80549-v

Cited by 24 publications

(13 citation statements)

References 20 publications

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“…Further confirmation that nigrin b is a RIP comes from the catalytic action of the protein against rRNA. Upon treatment with acid aniline, the isolated rRNA of RIP-inactivated ribosomes from mammalian [9], fungal [33] and bacterial ribosomes [13,14,30], released the so-called diagnostic RNA fragment. As shown in Fig.…”

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confidence: 99%

Isolation and partial characterization of nigrin b, a non-toxic novel type 2 ribosome-inactivating protein from the bark ofSambucus nigra L.

Girbés¹,

Citores

Ferreras

et al. 1993

Plant Mol Biol

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The bark of Sambucus nigra L. contains a non-toxic novel type 2 ribosome-inactivating protein that we named nigrin b. In vitro, nigrin b strongly inhibited mammalian protein synthesis but did not affect plant nor bacterial protein synthesis. The protein (M(r) 58,000) contains two subunits, A (M(r) 26,000) and B (M(r) 32,000); linked by disulphide bridge(s). Nigrin b was found to be an rRNA N-glycosidase of the rRNA of intact mammalian ribosomes and shares a very good N-terminal amino-acid sequence homology with the anti-HIV-1 proteins TAP 29 and trichosanthin.

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confidence: 99%

Isolation and partial characterization of nigrin b, a non-toxic novel type 2 ribosome-inactivating protein from the bark ofSambucus nigra L.

Girbés¹,

Citores

Ferreras

et al. 1993

Plant Mol Biol

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“…It was then found that MAP inhibited protein synthesis by E. coli ribosomes, although at concentrations some 100-fold higher than those affecting eukaryotic ribosomes (13). More recently it was reported that other type 1 RIPs, although at high concentrations, depurinate 23S rRNA of E. coli ribosomes (16,17,26).…”

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Effects of ribosome-inactivating proteins on Escherichia coli and Agrobacterium tumefaciens translation systems

et al. 1993

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The effects of 30 type 1 and of 2 (ricin and volkensin) type 2 ribosome-inactivating proteins (RIPs) on Escherichia coli and Agrobacterium tumefaciens cell-free translation systems were compared with the effects on a rabbit reticulocyte translation system. The depurinating activity of RIPs on E. coli ribosomes was also evaluated. Only six type 1 RIPs inhibited endogenous mRNA-directed translational activity of E. coli lysates, with submicromolar 50% inhibitory concentrations. Four RIPs had similar activities on poly(U)-directed phenylalanine polymerization by E. coli ribosomes, and three RIPs inhibited poly(U)-directed polyphenylalanine synthesis by A. tumefaciens ribosomes, with submicromolar 50%1 inhibitory concentrations.Ribosome-inactivating proteins (RIPs) from plants (reviewed in reference 34), either single-chain (type 1 RIPs) or two-chain (type 2 RIPs, i.e., ricin and related toxins), are N-glycosidases which hydrolyze the N-glycosidic bond of adenine in a highly conserved region of rRNA (7). As a result of this alteration, eukaryotic ribosomes become unable to bind elongation factors, with the consequent arrest of protein synthesis. On the other hand, protein synthesis by prokaryotic ribosomes is not significantly affected by ricin or other RIPs (4,5,12,18,25,29), and fully functional transgenic RIPs could be expressed in Escherichia coli (10,24,31). Nevertheless, at least ricin (8) and Mirabilis jalapa antiviral protein (MAP) (14) depurinate naked 23S and 16S E. coli rRNAs at A-2660 and at A-1014, respectively, and MAP could not be expressed at high levels in E. coli because of the toxicity of the protein to this organism (15). It was then found that MAP inhibited protein synthesis by E. coli ribosomes, although at concentrations some 100-fold higher than those affecting eukaryotic ribosomes (13). More recently it was reported that other type 1 RIPs, although at high concentrations, depurinate 23S rRNA of E. coli ribosomes (16,17,26).These results prompted us to study in a quantitative manner the activities of several RIPs on three prokaryote translation systems.Materials. E. coli MRE 600 was supplied by J. P. Ballesta, Madrid, Spain. Agrobacterium tumefaciens was obtained from the Departamento de Microbiologia, University of Valencia, Valencia, Spain.RIPs were purified from members of various plant families as follows: Caryophyllaceae, Dianthus caryophyllus leaves (dianthins), Lychnis chalcedonica seeds (lychnin), and Saponaria officinalis leaves (saporin-L proteins), roots (saporin-R), and seeds (saporin-S proteins); Cucurbitaceae, Bryonia dioica roots (bryodin-R), Citrullus colocynthis seeds (colocins), Momordica cochinchinensis seeds (momorcochin-S), Momordica charantia seeds (momordin 1), and Trichosanthes kirilowii seeds (trichokirin); Euphorbiaceae, Gelonium multiflorum seeds (gelo- Chloroacetaldehyde was prepared as described by McCann et al. (19). All other reagents were of analytical or molecular biology grade and, when possible, RNase free.Translation systems. Protein synthesis was determine...

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“…RIPs inhibit protein synthesis by mammalian, plant, protozoal, fungal and bacterial ribosomes [1,[7][8][9][10][11][12]. Very recently, it has been reported that saporin L1, an RIP from Saponaria officinalis L., displays depurinating activity on viral RNA and herring sperm DNA [13], which could account for the antiviral activity generally assigned to RIPs [14].…”

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confidence: 99%

Ebulitins: A new family of type 1 ribosome‐inactivating proteins (rRNA N‐glycosidases) from leaves of Sambucus ebulus L. that coexist with the type 2 ribosome‐inactivating protein ebulin 1

et al. 1995

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A new family of single chain (type 1) ribosome-inactivating proteins (RIPs), that we have named ebulitins, have been found in mature leaves of Sambucus ebulus L., a caprifoliaceae plant also known to contain a non-toxic two chain (type 2) RIP named ebulin 1 in its leaves. Ebulitins are basic proteins of Mr 32,000, 29,000 and 29,000 for ebulitins a,/3 and T, respectively. The simultaneous presence of different basic type 1 and acidic type 2 RIPs in the same plant and in the same tissue is described here for the first time and opens a new door in research into RIPs.

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Mechanism and site of action of a ribosome‐inactivating protein type 1 from Dianthus barbatus which inactivates Escherichia coli ribosomes

Cited by 24 publications

References 20 publications

Isolation and partial characterization of nigrin b, a non-toxic novel type 2 ribosome-inactivating protein from the bark ofSambucus nigra L.

Isolation and partial characterization of nigrin b, a non-toxic novel type 2 ribosome-inactivating protein from the bark ofSambucus nigra L.

Effects of ribosome-inactivating proteins on Escherichia coli and Agrobacterium tumefaciens translation systems

Ebulitins: A new family of type 1 ribosome‐inactivating proteins (rRNA N‐glycosidases) from leaves of Sambucus ebulus L. that coexist with the type 2 ribosome‐inactivating protein ebulin 1

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