plant ribosomes
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2021 ◽  
Vol 22 (3) ◽  
pp. 1434
Author(s):  
Pieter Wytynck ◽  
Jeroen Lambin ◽  
Simin Chen ◽  
Sinem Demirel Asci ◽  
Isabel Verbeke ◽  
...  

Ribosome-inactivating proteins (RIPs) are a class of cytotoxic enzymes that can inhibit protein translation by depurinating rRNA. Most plant RIPs are synthesized with a leader sequence that sequesters the proteins to a cell compartment away from the host ribosomes. However, several rice RIPs lack these signal peptides suggesting they reside in the cytosol in close proximity to the plant ribosomes. This paper aims to elucidate the physiological function of two nucleocytoplasmic RIPs from rice, in particular, the type 1 RIP referred to as OsRIP1 and a presumed type 3 RIP called nuRIP. Transgenic rice lines overexpressing these RIPs were constructed and studied for developmental effects resulting from this overexpression under greenhouse conditions. In addition, the performance of transgenic seedlings in response to drought, salt, abscisic acid and methyl jasmonate treatment was investigated. Results suggest that both RIPs can affect methyl jasmonate mediated stress responses.


Toxins ◽  
2019 ◽  
Vol 11 (6) ◽  
pp. 325 ◽  
Author(s):  
Jeroen De Zaeytijd ◽  
Pierre Rougé ◽  
Guy Smagghe ◽  
Els J.M. Van Damme

Ribosome-inactivating proteins (RIPs) are cytotoxic enzymes that inhibit protein translation by depurinating ribosomal RNA. Although most plant RIPs are synthesized with leader sequences that sequester them away from the host ribosomes, several RIPs from cereals lack these signal peptides and therefore probably reside in the cytosol near the plant ribosomes. More than 30 RIP genes have been identified in the rice (Oryza sativa spp. japonica) genome, many of them lacking a signal peptide. This paper focuses on a presumed cytosolic type-1 RIP from rice, referred to as OsRIP1. Using 3D modeling it is shown that OsRIP1 structurally resembles other cereal RIPs and has an active site that meets the requirements for activity. Furthermore, localization studies indicate that OsRIP1-eGFP fusion proteins reside in the nucleocytoplasmic space when expressed in epidermal cells of Nicotiana benthamiana or Arabidopsis thaliana suspension cells. Finally, OsRIP1 was recombinantly produced in Escherichia coli and was demonstrated to possess catalytic activity. Interestingly, this recombinant RIP inactivates wheat ribosomes far less efficiently than rabbit ribosomes in an in vitro system. These findings raise some interesting questions concerning the mode of action and physiological role of OsRIP1. This is the first time a RIP from rice is investigated at protein level and is shown to possess biological activity.


2013 ◽  
Vol 406 (6) ◽  
pp. 1629-1637 ◽  
Author(s):  
Leena Pitkänen ◽  
Päivi Tuomainen ◽  
Katri Eskelin

2010 ◽  
Vol 36 (3) ◽  
pp. 336-343 ◽  
Author(s):  
A. V. Zhigailov ◽  
D. M. Graifer ◽  
E. S. Babaylova ◽  
N. S. Polimbetova ◽  
G. G. Karpova ◽  
...  

2008 ◽  
Vol 18 (2) ◽  
pp. 175-186 ◽  
Author(s):  
Kamilla Bąkowska-Żywicka ◽  
Anna M. Kietrys ◽  
Tomasz Twardowski

1992 ◽  
Vol 20 (6) ◽  
pp. 1111-1119 ◽  
Author(s):  
Jiro Kataoka ◽  
Noriyuki Habuka ◽  
Masashi Miyano ◽  
Chikara Masuta ◽  
Akira Koiwai

FEBS Letters ◽  
1990 ◽  
Vol 273 (1-2) ◽  
pp. 144-146 ◽  
Author(s):  
Blair E. Taylor ◽  
James D. Irvin

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