The Structure and Action of Ribosome‐inactivating Proteins

Robertus, Jon D.; Monzingo, A.F.

doi:10.1002/9781118847237.ch8

Cited by 4 publications

(7 citation statements)

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“…Since type 2 RIP sequences are generally synthesized with a signal peptide, they follow the secretory route through the endoplasmic reticulum (ER)-Golgi pathway and finally after co-and posttranslational processing of the precursor including the cleavage of the signal peptide and the linker between the A and B domain accumulate in the plant vacuole or the intercellular space. The overall three-dimensional structure of all type 2 RIPs is very similar to the structure reported for ricin (Robertus and Monzingo 2014). Moreover the amino acid residues important for the catalytic site of the A chain and the sugar-binding sites of the B chain are highly conserved.…”

Section: Introductionmentioning

confidence: 63%

“…Each b-trefoil domain is composed of three subdomains (referred to as a, b, and g) showing a pseudothreefold symmetry, which assembles into a trefoil structure. Cocrystallization of ricin and its complementary carbohydrates revealed that the ricin B chain contains two carbohydrate binding subdomains, corresponding to the a-subdomain of the first b-trefoil domain and the g-subdomain of the second b-trefoil domain (Robertus and Monzingo 2014). In the case of ricin as well as for most type 2 RIPs the B chain specifically recognizes carbohydrate structures, such as galactose (Gal) and N-acetylgalactosamine (GalNAc).…”

Section: Introductionmentioning

confidence: 99%

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Plant AB Toxins with Lectin Domains

Shang¹,

Dang²,

Damme³

2015

Plant Toxins

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As part of their defense system different plant species each express a diverse set of defense proteins, among them proteins with lectin domains. The whole group of plant lectins assembles all proteins that have the ability to recognize and bind specific carbohydrate structures. Based on the sequence and the conformation of the carbohydrate recognition domains several lectin families are distinguished. Although many lectins are composed only of carbohydrate binding domains, several lectins are chimeric proteins composed of a lectin domain and another unrelated domain. In some cases this second domain can be considered as a toxin domain. This chapter focuses on different types of plant AB toxins and their physiological importance in the battle against pathogens and predators. Most information is available on type 2 ribosome-inactivating proteins in which an N-glycosidase domain is linked through a disulfide bridge to a lectin domain. More recently chimeric proteins consisting of one or more lectin domains and a dirigent domain or aerolysin domain have also been discovered. Although these AB toxins all consist of a lectin domain and a toxin domain, the nature of the toxin and the lectin domain are different resulting in proteins with different carbohydrate binding properties as well as a different mode of action for toxicity.

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Section: Introductionmentioning

confidence: 63%

Section: Introductionmentioning

confidence: 99%

Plant AB Toxins with Lectin Domains

Shang¹,

Dang²,

Damme³

2015

Plant Toxins

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“…Ricin is also by far the best studied RIP and can be considered as a representative model for the RIP family. To date the 3D structures of more than 20 RIPs, both A and AB forms, have been resolved and studied in detail [ 49 , 50 ].…”

Section: Biological Activity Of Cereal Rip Domainsmentioning

confidence: 99%

“…The structure of the A domain is highly conserved, irrespective of the domain architecture of the protein. While some authors suggest that the N-glycosidase domain consists of three domains [ 51 ], it is generally accepted that the A domain contains two subdomains [ 50 , 52 , 53 ]. The large N -terminal subdomain is composed of six α-helices and a six-stranded mixed β-sheet, and the small C -terminal subdomain consists of an anti-parallel β-sheet and an α-helix with a bend in the middle [ 49 ].…”

Section: Biological Activity Of Cereal Rip Domainsmentioning

confidence: 99%

Extensive Evolution of Cereal Ribosome-Inactivating Proteins Translates into Unique Structural Features, Activation Mechanisms, and Physiological Roles

Zaeytijd

Damme

2017

Toxins

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Ribosome-inactivating proteins (RIPs) are a class of cytotoxic enzymes that can depurinate rRNAs thereby inhibiting protein translation. Although these proteins have also been detected in bacteria, fungi, and even some insects, they are especially prevalent in the plant kingdom. This review focuses on the RIPs from cereals. Studies on the taxonomical distribution and evolution of plant RIPs suggest that cereal RIPs have evolved at an enhanced rate giving rise to a large and heterogeneous RIP gene family. Furthermore, several cereal RIP genes are characterized by a unique domain architecture and the lack of a signal peptide. This advanced evolution of cereal RIPs translates into distinct structures, activation mechanisms, and physiological roles. Several cereal RIPs are characterized by activation mechanisms that include the proteolytic removal of internal peptides from the N-glycosidase domain, a feature not documented for non-cereal RIPs. Besides their role in defense against pathogenic fungi or herbivorous insects, cereal RIPs are also involved in endogenous functions such as adaptation to abiotic stress, storage, induction of senescence, and reprogramming of the translational machinery. The unique properties of cereal RIPs are discussed in this review paper.

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“…It was reported that RIPs remove adenine from viral RNA, from DNA, and from the ADP-ribose chain of activated poly(ADP-ribose) polymerase (PARP), which led to propose the denomination of adenine polynucleotide glycosylase for RIPs. The matter is still controversial, because there are no studies on the kinetics with various substrates (Hartley and Lord 2004;Robertus and Monzingo 2014). On the other hand, several reports of various effects of RIPs (damage of cellular DNA, antiviral activity) independent of the inhibition of protein synthesis support the notion that RIPs may have other effect (s) than that on rRNA.…”

Section: Charybdin 1 29mentioning

confidence: 99%