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Author, Editor(s)

Author(s):

Tameling, Wladimir I.
Vossen, Jack H.
Albrecht, Mario
Lengauer, Thomas
Berden, Jan A.
Haring, Michel A.
Cornelissen, Ben J.C.
Takken, Frank L. W.

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Not MPG Author(s):

Tameling, Wladimir I.
Vossen, Jack H.
Berden, Jan A.
Haring, Michel A.
Cornelissen, Ben J.C.
Takken, Frank L.

BibTeX cite key*:

Albrecht2006b

Title

Title*:

Mutations in the NB-ARC domain of I-2 that impair ATP hydrolysis cause autoactivation

Journal

Journal Title*:

Plant Physiology

Journal's URL:


Download URL
for the article:

http://www.plantphysiol.org/cgi/reprint/140/4/1233

Language:

English

Publisher

Publisher's
Name:


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Address:


ISSN:


Vol, No, pp, Date

Volume*:

140

Number:

4

Publishing Date:

2006

Pages*:

1233-1245

Number of
VG Pages:


Page Start:


Page End:


Sequence Number:


DOI:


Note, Abstract, ©

Note:


(LaTeX) Abstract:

Resistance (R) proteins in plants confer specificity to the innate immune system. Most R proteins have a centrally located NB-ARC (nucleotide-binding adaptor shared by APAF-1, R proteins, and CED-4) domain. For two tomato (Lycopersicon esculentum) R proteins, I-2 and Mi-1, we have previously shown that this domain acts as an ATPase module that can hydrolyze ATP in vitro. To investigate the role of nucleotide binding and hydrolysis for the function of I-2 in planta, specific mutations were introduced in conserved motifs of the NB-ARC domain. Two mutations resulted in autoactivating proteins that induce a pathogen-independent hypersensitive response upon expression in planta. These mutant forms of I-2 were found to be impaired in ATP hydrolysis, but not in ATP binding, suggesting that the ATP- rather than the ADP-bound state of I-2 is the active form that triggers defense signaling. In addition, upon ADP binding, the protein displayed an increased affinity for ADP suggestive of a change of conformation. Based on these data, we propose that the NB-ARC domain of I-2, and likely of related R proteins, functions as a molecular switch whose state (on/off) depends on the nucleotide bound (ATP/ADP).

URL for the Abstract:

http://www.plantphysiol.org/cgi/content/abstract/140/4/1233

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Correlation

MPG Unit:

Max-Planck-Institut für Informatik



MPG Subunit:

Computational Biology and Applied Algorithmics

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BibTeX Entry:

@ARTICLE{Albrecht2006b,
AUTHOR = {Tameling, Wladimir I. and Vossen, Jack H. and Albrecht, Mario and Lengauer, Thomas and Berden, Jan A. and Haring, Michel A. and Cornelissen, Ben J.C. and Takken, Frank L. W.},
TITLE = {Mutations in the {NB-ARC} domain of {I-2} that impair {ATP} hydrolysis cause autoactivation},
JOURNAL = {Plant Physiology},
YEAR = {2006},
NUMBER = {4},
VOLUME = {140},
PAGES = {1233--1245},
}


Entry last modified by Uwe Brahm, 07/11/2007
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Editor(s)
Mario Albrecht
Created
03/23/2006 07:38:47 PM
Revisions
4.
3.
2.
1.
0.
Editor(s)
Uwe Brahm
Christine Kiesel
Mario Albrecht
Mario Albrecht
Mario Albrecht
Edit Dates
2007-07-11 12:32:00
22.02.2007 16:24:14
23.05.2006 20:09:44
23.03.2006 19:40:13
23.03.2006 19:38:47