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The tomato yellow leaf curl virus (TYLCV) V2 protein interacts with the host papain-like cysteine protease CYP1 -2012
Year:
2012
Source of publication :
Plant Signaling and Behavior
Authors :
Bar-Ziv, Amalia
;
.
Belausov, Eduard
;
.
Gafni, Yedidya
;
.
Hak, Hagit
;
.
Levy, Yael
;
.
Levy, Yoseph
;
.
Mett, Anahit
;
.
Volume :
7
Co-Authors:


Citovsky, V., Department of Biochemistry and Cell Biology, State University of New York, Stony Brook, NY, United States
 

Facilitators :
From page:
0
To page:
0
(
Total pages:
1
)
Abstract:
The V2 protein of Tomato yellow leaf curl geminivirus (TYLCV) is an RNA-silencing suppressor that counteracts the innate immune response of the host plant. However, this anti-host defense function of V2 may include targeting of other defensive mechanisms of the plant. Specifically, we show that V2 recognizes and directly binds the tomato CYP1 protein, a member of the family of papain-like cysteine proteases which are involved in plant defense against diverse pathogens. This binding occurred both in vitro and in vivo, within living plant cells. The V2 binding site within mCYP1 was identified in the direct proximity to the papain-like cysteine protease active site. © 2012 Landes Bioscience.
Note:
Related Files :
CYP1
Papain-like cysteine protease
Protein interaction
TYLCV
v2 protein
Show More
Related Content
More details
DOI :
10.4161/psb.20935
Article number:
0
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
19994
Last updated date:
02/03/2022 17:27
Creation date:
16/04/2018 23:33
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Scientific Publication
The tomato yellow leaf curl virus (TYLCV) V2 protein interacts with the host papain-like cysteine protease CYP1 -2012
7


Citovsky, V., Department of Biochemistry and Cell Biology, State University of New York, Stony Brook, NY, United States
 

The tomato yellow leaf curl virus (TYLCV) V2 protein interacts with the host papain-like cysteine protease CYP1
The V2 protein of Tomato yellow leaf curl geminivirus (TYLCV) is an RNA-silencing suppressor that counteracts the innate immune response of the host plant. However, this anti-host defense function of V2 may include targeting of other defensive mechanisms of the plant. Specifically, we show that V2 recognizes and directly binds the tomato CYP1 protein, a member of the family of papain-like cysteine proteases which are involved in plant defense against diverse pathogens. This binding occurred both in vitro and in vivo, within living plant cells. The V2 binding site within mCYP1 was identified in the direct proximity to the papain-like cysteine protease active site. © 2012 Landes Bioscience.
Scientific Publication
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