JIP60-mediated, jasmonate- and senescence-induced molecular switch in translation toward stress and defense protein synthesis

Rustgi, Sachin; Pollmann, Stephan; Buhr, Frank; Springer, Armin; Reinbothe, Christiane; Wettstein, Diter von; Reinbothe, Steffen

doi:10.1073/pnas.1415690111

Cited by 37 publications

(44 citation statements)

References 45 publications

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“…As described earlier, JIP60 is a 60 kDa jasmonate-inducible chimeric protein that consists of an N -terminal RIP domain and a C -terminal domain which displays similarity to eukaryotic translation initiation factor 4E [37,70]. Like maize RIP1, JIP60 differs from other RIPs in containing internal acidic peptides of 20–25 amino acids that will be removed during maturation of the protein.…”

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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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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“…Therefore, any modifications in this fragment of 25S rRNA lead to the inactivation of the large ribosomal subunit and cessation of protein synthesis during the elongation step (Dunaeva et al 1999;Sawasaki et al 2008). JIP60 also plays a key role in inhibiting cytoplasmic protein synthesis via reversible ribosome dissociation into small and large subunits (Reinbothe et al 1994;Rustgi et al 2014). Some authors have suggested that the upregulation of JIP60 during salinity stress inhibits growth (Görschen et al 1995) and protects plants against stress.…”

Section: Signal Transduction Transcription and Translation Processingmentioning

confidence: 99%

ABA pretreatment can limit salinity-induced proteome changes in growing barley sprouts

2017

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A proteomic study was conducted on caryopses of barley cv. Stratus (Hordeum vulgare). The caryopses were germinated in darkness at 20°C, according to one of the three experimental setups: (a) in distilled water for 24 h, followed by 100 mM NaCl for another 24 h (salinity stress, SS); (b) in 100 lM abscisic acid for 24 h, with rinsing in distilled water to remove residual ABA, followed by 100 mM NaCl for another 24 h (pretreatment with ABA ? salinity stress, ABAS); and (c) only in distilled water, for comparison with the tested samples (control, C). After 48 h, proteomes were extracted from barley sprouts in each treatment, according to the method by Gallardo et al. (2002a, b, modified). Proteins were then separated by 2DE and analyzed by MALDI-TOF/MS (Bruker). Under salinity stress, we observed changes in the pattern of proteins involved in: (a) energy metabolism, (b) one-carbon metabolism, (c) cell wall biogenesis, lignification, and adhesion, (d) response to oxidative stress, desiccation stress, and other defense responses, (e) structure and organization of the cytoskeleton, (f) signal transduction, transcription and translation processing, and (g) protein turnover. Our results revealed that ABA can alter the response of barley seedlings to salinity stress. In general, ABA pretreatment limited stress-induced proteomic changes. Alterations in energy and one-carbon metabolism indicate the importance of ABA in glycolytic/gluconeogenic pathways and the SMM cycle during salinity stress. Other observations demonstrated the role of ABA in hemicellulose, cellulose and lignin biosynthesis, ROS scavenging, actin CK formation, control of PI signaling, chromatin-mediated mechanism of stress tolerance, mRNA stability, and protection against dehydration.

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“…One example is the JIP60 protein (60 kDa jasmonate-induced protein) found in barley (Chaudhry et al, 1994). This is a chimeric protein where a RIP domain is linked to a domain which has similarity to the eukaryotic translation initiation factor 4E (Rustgi et al, 2014).…”

Section: Ribosome-inactivating Proteinsmentioning

confidence: 99%

Toxic proteins in plants

2015

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Plants have evolved to synthesize a variety of noxious compounds to cope with unfavorable circumstances, among which a large group of toxic proteins that play a critical role in plant defense against predators and microbes. Up to now, a wide range of harmful proteins have been discovered in different plants, including lectins, ribosome-inactivating proteins, protease inhibitors, ureases, arcelins, antimicrobial peptides and pore-forming toxins. To fulfill their role in plant defense, these proteins exhibit various degrees of toxicity towards animals, insects, bacteria or fungi. Numerous studies have been carried out to investigate the toxic effects and mode of action of these plant proteins in order to explore their possible applications. Indeed, because of their biological activities, toxic plant proteins are also considered as potentially useful tools in crop protection and in biomedical applications, such as cancer treatment. Genes encoding toxic plant proteins have been introduced into crop genomes using genetic engineering technology in order to increase the plant's resistance against pathogens and diseases. Despite the availability of ample information on toxic plant proteins, very few publications have attempted to summarize the research progress made during the last decades. This review focuses on the diversity of toxic plant proteins in view of their toxicity as well as their mode of action. Furthermore, an outlook towards the biological role(s) of these proteins and their potential applications is discussed.

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JIP60-mediated, jasmonate- and senescence-induced molecular switch in translation toward stress and defense protein synthesis

Cited by 37 publications

References 45 publications

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

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

ABA pretreatment can limit salinity-induced proteome changes in growing barley sprouts

Toxic proteins in plants

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