Ribosome-inactivating proteins in edible plants and purification and characterization of a new ribosome-inactivating protein from Cucurbita moschata

Barbieri, Luigi; Polito, Letizia; Bolognesi, Andrea; Ciani, Marialibera; Pelosi, Emanuele; Farini, Valentina; Jha, Ajay Kumar; Sharma, Neelam; Vivanco, Jorge M.; Parente, Augusto; Stirpe, Fiorenzo

doi:10.1016/j.bbagen.2006.01.002

Cited by 77 publications

(44 citation statements)

References 60 publications

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“…The other RIPs included in the comparison have Ile, Val or Ala at the N-terminus, which may be related to remarkable diVerential in vivo stabilities (Ile, 20 h;Val, 100 h;Ala, 4 h and N, 1.4 h;Varshavsky 1997). Furthermore, the amino acid residues involved in the formation of the active site (i.e., Tyr73, Tyr121, Glu176, Arg179, Trp210), and those reported as invariant at the RIP N-terminus (Tyr14, Phe17, Arg22; Barbieri et al 2006), are fully conserved. The identity/similarity matrix revealed that dioicin 2 exhibits the highest percentage identity (81.6%) and similarity (84.6%) with PAP-II, type 1 RIP isolated from early summer leaves of P. americana (Fig.…”

Section: Amino Acid Sequence Of Dioicin 2 and Cysteinyl Pairingmentioning

confidence: 97%

Type 1 ribosome-inactivating proteins from Phytolacca dioica L. leaves: differential seasonal and age expression, and cellular localization

Parente¹,

Conforto

Maro³

et al. 2008

Planta

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The expression of type 1 ribosome-inactivating proteins (RIPs) in Phytolacca dioica L. leaves was investigated. Fully expanded leaves of young P. dioica plants (up to 3 years old) expressed two novel RIPs, dioicin 1 and dioicin 2. The former was also found in developing leaves from adult P. dioica within about two and a half weeks after leaf development, and the latter continuously synthesized, with no seasonal or ontogenetic constraint. Fully expanded leaves from adult P. dioica expressed four RIPs (PD-Ls1-4) exhibiting seasonal variation. RIPs were localized in the extracellular space, in the vacuole and in the Golgi apparatus of mesophyll cells. Dioicin 1 and dioicin 2 showed rRNA N-beta-glycosidase activity and displayed the following properties, respectively: (1) Mr values of 30,047.00 and 29,910.00, (2) pIs of 8.74 and 9.37, and (3) IC(50) values of 19.74 (0.658 nM) and 6.85 ng/mL (0.229 nM). Furthermore, they showed adenine polynucleotide glycosylase activity and nicked pBR322 dsDNA. The amino acid sequence of dioicin 2 had 266 amino acid residues, and the highest percentage identity (81.6%) and similarity (84.6%) with PAP-II from Phytolacca americana, while its identity with other RIPs from Phytolaccaceae was around 40%.

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Section: Amino Acid Sequence Of Dioicin 2 and Cysteinyl Pairingmentioning

confidence: 97%

Type 1 ribosome-inactivating proteins from Phytolacca dioica L. leaves: differential seasonal and age expression, and cellular localization

Parente¹,

Conforto

Maro³

et al. 2008

Planta

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“…These results indicate the occurrence of an early direct damage to DNA, independent of the inhibition of protein synthesis, and suggest that these toxins may enter the nucleus. [63], porrectin, from C. porrectum [64], a RIPtype protein from tobacco [65] and a RIP from Cucurbita moschata [19] have been reported to have SOD activity at a level that seemed to exclude the possibility of contamination. Purified SOD was also reported to have RIP activity [65] and the tobacco protein had a sequence similar to that of SOD, thus leading to the hypothesis that the two proteins had dual enzymatic activity.…”

Section: Enzymatic Activitymentioning

confidence: 97%

“…Allergy to elderberry has also been attributed to a protein with the characteristics of a type 1 RIP [143]. Since RIPs are present in plants that are eaten raw [5,19], their allergenic properties may have a role in the pathogenesis of the allergies caused by some vegetables.…”

Section: Allergiesmentioning

confidence: 97%

Ribosome-inactivating proteins: progress and problems

Stirpe

Battelli

2006

Cell. Mol. Life Sci.

318

225

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Ribosome-inactivating proteins (RIPs), mostly from plants, are enzymes which depurinate rRNA, thus inhibiting protein synthesis. They also depurinate other polynucleotide substrates. The biological activity of RIPs is not completely clarified, and sometimes independent of the inhibition of protein synthesis. There are differences in the cytotoxicity of RIPs and, consequently, in their toxicity to animals. Some RIPs are potent toxins, the best known being ricin, a potential biological weapon. New toxins have recently been identified. RIPs cause apoptotic and necrotic lesions, and induce production of cytokines causing inflammation. RIPs are potentially useful in agriculture and medicine because (i) they have antiviral activity and (ii) they are used for the preparation of conjugates with antibodies ('immunotoxins') or other carriers, rendering them specifically toxic to the cell target of the carrier, which may be helpful in therapy. The distribution, mechanism of action and role in nature of RIPs are not completely understood, and we can expect several future developments in their practical application.

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“…Besides this, RIPs have also been suggested to process nuclease (Peumans et al 2001) and superoxide dismutase (SOD) activities (Li et al 1996(Li et al , 1997Sharma et al 2004; Barbieri et al 2006). However, no conclusive results were reported about these activities.…”

Section: Introductionmentioning

confidence: 97%

Genome-wide survey of the RIP domain family in Oryza sativa and their expression profiles under various abiotic and biotic stresses

et al. 2008

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Ribosome-inactivating proteins (RIPs) are N-glycosidases that inhibit protein synthesis by depurinating rRNA. Despite their identification more than 25 years ago, little is known about their biological functions. Here, we report a genome-wide identification of the RIP family in rice based on the complete genome sequence analysis. Our data show that rice genome encodes at least 31 members of this family and they all belong to type 1 RIP genes. This family might have evolved in parallel to species evolution and genome-wide duplications represent the major mechanism for this family expansion. Subsequently, we analyzed their expression under biotic (bacteria and fungus infection), abiotic (cold, drought and salinity) and the phytohormone ABA treatment. These data showed that some members of this family were expressed in various tissues with differentiated expression abundances whereas several members showed no expression under normal growth conditions or various environmental stresses. On the other hand, the expression of many RIP members was regulated by various abiotic and biotic stresses. All these data suggested that specific members of the RIP family in rice might play important roles in biotic and abiotic stress-related biological processes and function as a regulator of various environmental cues and hormone signaling. They may be potentially useful in improving plant tolerance to various abiotic and biotic stresses by over-expressing or suppressing these genes.

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Ribosome-inactivating proteins in edible plants and purification and characterization of a new ribosome-inactivating protein from Cucurbita moschata

Cited by 77 publications

References 60 publications

Type 1 ribosome-inactivating proteins from Phytolacca dioica L. leaves: differential seasonal and age expression, and cellular localization

Type 1 ribosome-inactivating proteins from Phytolacca dioica L. leaves: differential seasonal and age expression, and cellular localization

Ribosome-inactivating proteins: progress and problems

Genome-wide survey of the RIP domain family in Oryza sativa and their expression profiles under various abiotic and biotic stresses

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