Avirulence protein 3a (AVR3a) from the potato pathogen Phytophthora infestans forms homodimers through its predicted translocation region and does not specifically bind phospholipids

Stephan Wawra; Mark Agacan; Justin A. Boddey; Ian Davidson; Claire M.M. Gachon; Matteo Zanda; Severine Grouffaud; Stephen C. Whisson; Paul R.J. Birch; A.J. Porter; Pieter Van West

doi:10.1074/jbc.M112.395129

Avirulence protein 3a (AVR3a) from the potato pathogen Phytophthora infestans forms homodimers through its predicted translocation region and does not specifically bind phospholipids

Stephan Wawra, Mark Agacan, Justin A. Boddey, Ian Davidson, Claire M.M. Gachon, Matteo Zanda, Severine Grouffaud, Stephen C. Whisson, Paul R.J. Birch, A.J. Porter, Pieter Van West

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

30 Citations (Scopus)

Abstract

Background: AVR3a is a Phytophthora infestans effector that translocates into potato cells dependent on the N-terminal RxLR leader. Results: AVR3a dimerization is inhibited by a mutation that also impairs translocation. Conclusion: Phospholipid binding of AVR3a is probably physiologically irrelevant because only denatured protein molecules bind. Significance: Our findings will help us to understand how oomycete RxLR effectors function.

Original language	English
Pages (from-to)	38101-38109
Number of pages	9
Journal	Journal of Biological Chemistry
Volume	287
Issue number	45
DOIs	https://doi.org/10.1074/jbc.M112.395129
Publication status	Published - 2012

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10.1074/jbc.M112.395129

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Wawra, S., Agacan, M., Boddey, J. A., Davidson, I., Gachon, C. M. M., Zanda, M., Grouffaud, S., Whisson, S. C., Birch, P. R. J., Porter, A. J., & Van West, P. (2012). Avirulence protein 3a (AVR3a) from the potato pathogen Phytophthora infestans forms homodimers through its predicted translocation region and does not specifically bind phospholipids. Journal of Biological Chemistry, 287(45), 38101-38109. https://doi.org/10.1074/jbc.M112.395129

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title = "Avirulence protein 3a (AVR3a) from the potato pathogen Phytophthora infestans forms homodimers through its predicted translocation region and does not specifically bind phospholipids",

abstract = "Background: AVR3a is a Phytophthora infestans effector that translocates into potato cells dependent on the N-terminal RxLR leader. Results: AVR3a dimerization is inhibited by a mutation that also impairs translocation. Conclusion: Phospholipid binding of AVR3a is probably physiologically irrelevant because only denatured protein molecules bind. Significance: Our findings will help us to understand how oomycete RxLR effectors function.",

author = "Stephan Wawra and Mark Agacan and Boddey, {Justin A.} and Ian Davidson and Gachon, {Claire M.M.} and Matteo Zanda and Severine Grouffaud and Whisson, {Stephen C.} and Birch, {Paul R.J.} and A.J. Porter and {Van West}, Pieter",

year = "2012",

doi = "10.1074/jbc.M112.395129",

language = "English",

volume = "287",

pages = "38101--38109",

journal = "Journal of Biological Chemistry",

issn = "0021-9258",

publisher = "American Society for Biochemistry and Molecular Biology Inc.",

number = "45",

}

Wawra, S, Agacan, M, Boddey, JA, Davidson, I, Gachon, CMM, Zanda, M, Grouffaud, S, Whisson, SC, Birch, PRJ, Porter, AJ & Van West, P 2012, 'Avirulence protein 3a (AVR3a) from the potato pathogen Phytophthora infestans forms homodimers through its predicted translocation region and does not specifically bind phospholipids', Journal of Biological Chemistry, vol. 287, no. 45, pp. 38101-38109. https://doi.org/10.1074/jbc.M112.395129

Avirulence protein 3a (AVR3a) from the potato pathogen Phytophthora infestans forms homodimers through its predicted translocation region and does not specifically bind phospholipids. / Wawra, Stephan; Agacan, Mark; Boddey, Justin A. et al.
In: Journal of Biological Chemistry, Vol. 287, No. 45, 2012, p. 38101-38109.

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

TY - JOUR

T1 - Avirulence protein 3a (AVR3a) from the potato pathogen Phytophthora infestans forms homodimers through its predicted translocation region and does not specifically bind phospholipids

AU - Wawra, Stephan

AU - Agacan, Mark

AU - Boddey, Justin A.

AU - Davidson, Ian

AU - Gachon, Claire M.M.

AU - Zanda, Matteo

AU - Grouffaud, Severine

AU - Whisson, Stephen C.

AU - Birch, Paul R.J.

AU - Porter, A.J.

AU - Van West, Pieter

PY - 2012

Y1 - 2012

N2 - Background: AVR3a is a Phytophthora infestans effector that translocates into potato cells dependent on the N-terminal RxLR leader. Results: AVR3a dimerization is inhibited by a mutation that also impairs translocation. Conclusion: Phospholipid binding of AVR3a is probably physiologically irrelevant because only denatured protein molecules bind. Significance: Our findings will help us to understand how oomycete RxLR effectors function.

AB - Background: AVR3a is a Phytophthora infestans effector that translocates into potato cells dependent on the N-terminal RxLR leader. Results: AVR3a dimerization is inhibited by a mutation that also impairs translocation. Conclusion: Phospholipid binding of AVR3a is probably physiologically irrelevant because only denatured protein molecules bind. Significance: Our findings will help us to understand how oomycete RxLR effectors function.

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DO - 10.1074/jbc.M112.395129

M3 - Article

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SN - 0021-9258

VL - 287

SP - 38101

EP - 38109

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 45

ER -

Avirulence protein 3a (AVR3a) from the potato pathogen Phytophthora infestans forms homodimers through its predicted translocation region and does not specifically bind phospholipids

Abstract

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Aref#d: 20586. What are the Roles of Oomycete RXLR Effectors in the Establishment of Plant Disease? (joint with Warwick University). Was CO0221

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Avirulence protein 3a (AVR3a) from the potato pathogen Phytophthora infestans forms homodimers through its predicted translocation region and does not specifically bind phospholipids

Abstract

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Projects

Aref#d: 20586. What are the Roles of Oomycete RXLR Effectors in the Establishment of Plant Disease? (joint with Warwick University). Was CO0221

Cite this