scholarly journals Localization of the type I ribosome-inactivating protein, luffin, in adult and embryonic tissues of Luffa cylindrica L. Roem.

1999 ◽  
Vol 50 (334) ◽  
pp. 573-579
Author(s):  
A. Di Cola ◽  
G. Marcozzi ◽  
R. Balestrini ◽  
L. Spano
1992 ◽  
Vol 19 (5) ◽  
pp. 887-889 ◽  
Author(s):  
Jiro Kataoka ◽  
Noriyuki Habuka ◽  
Masashi Miyano ◽  
Chikara Masuta ◽  
Akira Koiwai

2009 ◽  
Vol 18 (2) ◽  
pp. 161-172 ◽  
Author(s):  
Ou Sha ◽  
David Tai-Wai Yew ◽  
Eric Yu-Pang Cho ◽  
Tzi-Bun Ng ◽  
Lin Yuan ◽  
...  

2012 ◽  
Vol 68 (11) ◽  
pp. 1488-1500 ◽  
Author(s):  
Byung-Gil Lee ◽  
Min Kyung Kim ◽  
Byeong-Won Kim ◽  
Se Won Suh ◽  
Hyun Kyu Song

Ribosome-inactivating protein (RIP), a defence protein found in various plants, possesses different chain architectures and activation mechanisms. The RIP from barley (bRIP) is a type I RIP and has sequence features that are divergent from those of type I and type II RIPs from dicotyledonous plants and even the type III RIP from maize. This study presents the first crystal structure of an RIP from a cereal crop, barley, in free, AMP-bound and adenine-bound states. For phasing, a codon-optimized syntheticbrip1gene was used and a vector was constructed to overexpress soluble bRIP fusion proteins; such expression has been verified in a number of cases. The overall structure of bRIP shows folding similar to that observed in other RIPs but also shows significant differences in specific regions, particularly in a switch region that undergoes a structural transition between a 310-helix and a loop depending on the liganded state. The switch region is in a position equivalent to that of a proteolytically susceptible and putative ribosome-binding site in type III RIPs. Thus, the bRIP structure confirms the detailed enzymatic mechanism of this N-glycosidase and reveals a novel activation mechanism for type I RIPs from cereal crops.


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