Ebulin 1, a nontoxic novel type 2 ribosome-inactivating protein from Sambucus ebulus L. leaves.

@article{Girbs1993Ebulin1A,
  title={Ebulin 1, a nontoxic novel type 2 ribosome-inactivating protein from Sambucus ebulus L. leaves.},
  author={Tom{\'a}s Girb{\'e}s and Luc{\'i}a Citores and R. Iglesias and Jos{\'e} Miguel Ferreras and Raquel Muñoz and M Angeles Rojo and Francisco Javier Arias and J. Rodr{\'i}guez Garc{\'i}a and Enrique Méndez and M Calonge},
  journal={The Journal of biological chemistry},
  year={1993},
  volume={268 24},
  pages={
          18195-9
        }
}
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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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The presence in fruits of elder of a new non-toxic type 2 RIP (nigrin f) that co-exists with a lectin known as SNA IV is described, demonstrating close homology of the catalytic A chain with type 1 RIPs, especially those from Cucurbitaceae and the B chain with several lectins previously isolated from Sambucus species.

Structure and Biological Properties of Ribosome-Inactivating Proteins and Lectins from Elder (Sambucus nigra L.) Leaves

The diversity of RIPs and lectins in the different elderberry tissues, and the different biological activities of these proteins, constitute an excellent source of proteins that are of great interest in diagnostics, experimental therapy, and agriculture.

Ribosome-inactivating proteins (RNA N-glycosidases) from the seeds of Saponaria ocymoides and Vaccaria pyramidata.

Two proteins were purified which have the properties of the type-1 (single-chain) ribosome-inactivating proteins of the Caryophyllaceae Saponaria ocymoides and Vaccaria pyramidata.

2.8‐Å crystal structure of a nontoxic type‐II ribosome‐inactivating protein, ebulin l

Ebulin l is shown to bind an A‐chain substrate analogue, pteroic acid, in the same manner as ricin, and is considered a nontoxic type‐II RIP due to a reduced cytotoxicity on whole cells and animals as compared with other toxic type‐ II RIP like ricin.

Cinnamomin--a versatile type II ribosome-inactivating protein.

Understanding of cinnamomin and the relative new proteins will help expand the knowledge of RIPs and may accelerate theoretical study and the development of their potential applications.

Sambucus Ribosome-Inactivating Proteins and Lectins

The main findings about structural features and biological activities of these proteins as well as the evolutionary relationship between them and some of their potential uses are presented.

Isolation and characterization of four type-1 ribosome-inactivating proteins, with polynucleotide:adenosine glycosidase activity, from leaves of Phytolacca dioica L.

Four type-1 (single-chain) ribosome-inactivating proteins (RIPs) isolated from leaves of Phytolacca dioica L produced the β-fragment, diagnostic of the specific enzymatic action of RIPs, on yeast ribosomes, thus acting as polynucleotide:adenosine glycosidases.

New ribosome-inactivating proteins and other proteins with protein synthesis–inhibiting activities

New/unusual RIPs discussed in the present review encompass metazoan RIPs from Anopheles and Culex mosquitos, antimicrobial peptides derived from RIP of the pokeweed Phytolacca dioica, maize RIP (a type III RIP derived from a precursor form), RIPs with a molecular weight smaller than those of regular type 1 RIPs are produced by plants in the Cucurbitaceae family.

Presence of polymerized and free forms of the non-toxic type 2 ribosome-inactivating protein ebulin and a structurally related new homodimeric lectin in fruits of Sambucus ebulus L.

Polymerization of ebulin and the dimeric lectin may represent a novel means of storing the non-toxic type 2 ribosome-inactivating proteins and lectins found in highly metabolic tissues, such as green fruits.
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