Imperial College London
Alternate

ProfessorPietroSpanu

Faculty of Natural Sciences, Department of Life Sciences

Professor of Molecular Plant Pathology
 
 
 
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Contact

 

+44 (0)20 7594 5384p.spanu Website

 
 
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Location

 

610Sir Alexander Fleming BuildingSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{Spanu:2020:10.1104/pp.19.01029,
author = {Spanu, P and Przydacz, M and Jones, R and Pennington, H and Belmans, G and Bruderer, M and Greenhill, R and Salter, T and Wellham, P and Cota, E},
doi = {10.1104/pp.19.01029},
journal = {Plant Physiology},
title = {Mode of action of the catalytic site in the N-terminal ribosome-inactivating domain of barley JIP60},
url = {http://dx.doi.org/10.1104/pp.19.01029},
year = {2020}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - Jasmonate-induced protein 60 (JIP60) is a ribosome-inactivating protein from barley (Hordeum vulgare) and is involved in the plant immune response dependent on the jasmonate hormones. Here, we demonstrate that transient expression in Nicotiana benthamiana of the N-terminal domain of JIP60, from which the inhibitor domain (amino acids 163 to 185) is removed, initiates cell death leading to extensive necrosis of leaf tissues. We used structure prediction of JIP60 to identify potential catalytic amino acids in the active site and tested these by mutagenesis and in planta assays of necrosis induction by expression in N. benthamiana, as well as through an in vitro translation-inactivation assay. We found that Tyrosine 96, Glutamate 202, Arginine 205, and Tryptophan 235 in the presumptive active site of JIP60 are conserved in 815 plant ribosome inactivating proteins (RIP) in the Pfam database identified using HMMER as containing a RIP domain. When these amino acid residues are individually mutated, the necrosis-inducing activity is completely abolished. We therefore propose a role for these amino acids in JIP60 activity (depurination of adenosine in ribosomes). This study provides insight into the catalytic mechanism of this protein.
AU  - Spanu,P
AU  - Przydacz,M
AU  - Jones,R
AU  - Pennington,H
AU  - Belmans,G
AU  - Bruderer,M
AU  - Greenhill,R
AU  - Salter,T
AU  - Wellham,P
AU  - Cota,E
DO  - 10.1104/pp.19.01029
PY  - 2020///
SN  - 0032-0889
TI  - Mode of action of the catalytic site in the N-terminal ribosome-inactivating domain of barley JIP60
T2  - Plant Physiology
UR  - http://dx.doi.org/10.1104/pp.19.01029
UR  - http://www.plantphysiol.org/content/early/2020/03/02/pp.19.01029
ER  -
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