Isolation and characterization of two new N-glycosidase type-1 ribosome-inactivating proteins, unrelated in amino-acid sequence, from Petrocoptis species

@article{Arias1994IsolationAC,
  title={Isolation and characterization of two new N-glycosidase type-1 ribosome-inactivating proteins, unrelated in amino-acid sequence, from Petrocoptis species},
  author={Francisco Javier Arias and Mar{\'i}a Angeles Rojo and Jos{\'e} Miguel Ferreras and Rosario Iglesias and Raquel Muñoz and Fernando Soriano and Enrique Méndez and Luigi Barbieri and Tom{\'a}s Girb{\'e}s},
  journal={Planta},
  year={1994},
  volume={194},
  pages={487-491}
}
Two new N-glycosidase type-1 ribosome-inactivating proteins (RIPs), denoted petroglaucin 1 and petrograndin, respectively, were isolated from the plantsPetrocoptis glaucifolia (Lag.) Boiss sp.viscosa (Rothm.) Laínz andPetrocoptis grandiflora Rothm. These new RIPs do not share H2N-terminal amino-acid sequence homology with petroglaucin (now denoted as petroglaucin 2), the only other type-1 RIP to be isolated fromP. glaucifolia (Arias et al. (1992) Planta186, 532–540). Petroglaucin 1 shares amino… 

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References

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Isolation and partial characterization of a new ribosome-inactivating protein from Petrocoptis glaucifolia (Lag.) Boiss

The total activity of this translational inhibitor has been found to increase up to 11-fold during its purification, indicating that some regulatory factor that normally blocks the translational inhibitory activity of the ribosome-inactivating protein in crude extracts of the plant is removed during purification.

Type 1 ribosome-inactivating proteins depurinate plant 25S rRNA without species specificity.

It is demonstrated that plant ribosomes are generally susceptible to RIP attack, including modification by their own RIPs, as well as from the plant species from which the particular RIP had been isolated.

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

The bark of Sambucus nigra L contains a non-toxic novel type 2 ribosome-inactivating protein that is 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.

Effect of alpha-sarcin and ribosome-inactivating proteins on the interaction of elongation factors with ribosomes.

The effect of alpha-sarcin and that of RIPs on the interaction of elongation factors with Artemia salina (brine shrimp) ribosomes have been investigated and four proteins tested have, however, a comparable activity on the rabbit reticulocyte-lysate system.

The complete amino acid sequence of momordin-a, a ribosome-inactivating protein from the seeds of bitter gourd (Momordica charantia).

The sequence comparison with ricin A-chain shows that 33% of the residues of momordin-a are identical to those of ricin C-chain and that the residues involved in the catalytic site of the ricin B-chain are conserved in momord in-a.

Complete amino acid sequence of luffin-a, a ribosome-inactivating protein from the seeds of sponge gourd (Luffa cylindrica).

The complete amino acid sequence of luffin-a has been determined and a comparison with the sequence of ricin A-chain showed 33% sequence identity indicating that these proteins are homologous.