The N-terminal domain of the tomato immune protein prf contains multiple homotypic and pto kinase interaction sites

Isabel Marie Luise Saur; Brendon Francis Conlan; John Paul Rathjen

doi:10.1074/jbc.M114.616532

The N-terminal domain of the tomato immune protein prf contains multiple homotypic and pto kinase interaction sites

Isabel Marie Luise Saur
, Brendon Francis Conlan
, John Paul Rathjen^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

24 Citations (Scopus)

Abstract

Background: Plant immune proteins display complex conformations. Results: The Prf N-terminal domain forms a homo-dimer, has two binding sites for Pto kinase, and interacts with the Prf leucine-rich repeats domain. Conclusion: The Prf N-terminal domain coordinates multiple domain interactions to control the activity of the immune complex. Significance: Additional resolution is supplied to the Prf-Pto complex.

Original language	English
Pages (from-to)	11258-11267
Number of pages	10
Journal	Journal of Biological Chemistry
Volume	290
Issue number	18
DOIs	https://doi.org/10.1074/jbc.M114.616532
Publication status	Published - 1 May 2015

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10.1074/jbc.M114.616532

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title = "The N-terminal domain of the tomato immune protein prf contains multiple homotypic and pto kinase interaction sites",

abstract = "Background: Plant immune proteins display complex conformations. Results: The Prf N-terminal domain forms a homo-dimer, has two binding sites for Pto kinase, and interacts with the Prf leucine-rich repeats domain. Conclusion: The Prf N-terminal domain coordinates multiple domain interactions to control the activity of the immune complex. Significance: Additional resolution is supplied to the Prf-Pto complex.",

author = "Saur, \{Isabel Marie Luise\} and Conlan, \{Brendon Francis\} and Rathjen, \{John Paul\}",

note = "Publisher Copyright: {\textcopyright} 2015 by The American Society for Biochemistry and Molecular Biology, Inc.",

year = "2015",

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doi = "10.1074/jbc.M114.616532",

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T1 - The N-terminal domain of the tomato immune protein prf contains multiple homotypic and pto kinase interaction sites

AU - Saur, Isabel Marie Luise

AU - Conlan, Brendon Francis

AU - Rathjen, John Paul

PY - 2015/5/1

Y1 - 2015/5/1

N2 - Background: Plant immune proteins display complex conformations. Results: The Prf N-terminal domain forms a homo-dimer, has two binding sites for Pto kinase, and interacts with the Prf leucine-rich repeats domain. Conclusion: The Prf N-terminal domain coordinates multiple domain interactions to control the activity of the immune complex. Significance: Additional resolution is supplied to the Prf-Pto complex.

AB - Background: Plant immune proteins display complex conformations. Results: The Prf N-terminal domain forms a homo-dimer, has two binding sites for Pto kinase, and interacts with the Prf leucine-rich repeats domain. Conclusion: The Prf N-terminal domain coordinates multiple domain interactions to control the activity of the immune complex. Significance: Additional resolution is supplied to the Prf-Pto complex.

UR - https://www.scopus.com/pages/publications/84929500822

U2 - 10.1074/jbc.M114.616532

DO - 10.1074/jbc.M114.616532

M3 - Article

SN - 0021-9258

VL - 290

SP - 11258

EP - 11267

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 18

ER -

The N-terminal domain of the tomato immune protein prf contains multiple homotypic and pto kinase interaction sites

Abstract

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