Hydrogen peroxide is a regulator of ABI1, a protein phosphatase 2C from Arabidopsis

Michael Meinhard; Erwin Grill

doi:10.1016/S0014-5793(01)03106-4

Hydrogen peroxide is a regulator of ABI1, a protein phosphatase 2C from Arabidopsis

Michael Meinhard, Erwin Grill

Chair of Botany

Technical University of Munich

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

176 Scopus citations

Abstract

Protein phosphatases 2C (PP2Cs) exhibit diverse regulatory functions in signalling pathways of animals, yeast and plants. ABI1 is a PP2C of Arabidopsis that exerts negative control on signalling of the phytohormone abscisic acid (ABA). Characterisation of the redox sensitivity of ABI1 revealed a strong enzymatic inactivation by hydrogen peroxide (H₂O₂) which has recently been implicated as a secondary messenger of ABA signalling. H₂O₂ reversibly inhibited ABI1 activity in vitro with an IC₅₀ of approximately 140 μM in the presence of physiological concentrations of glutathione. In addition, ABI1 was highly susceptible to inactivation by phenylarsine oxide (IC₅₀=3-4 μM) indicative for the facile oxidation of vicinal cysteine residues. Thus, H₂O₂ generated during ABA signalling seems to inactivate the negative regulator of the ABA response.

Original language	English
Pages (from-to)	443-446
Number of pages	4
Journal	FEBS Letters
Volume	508
Issue number	3
DOIs	https://doi.org/10.1016/S0014-5793(01)03106-4
State	Published - 23 Nov 2001

Keywords

Abscisic acid
Arabidopsis
Plant hormone
Protein phosphatase 2C
Signalling

Access to Document

10.1016/S0014-5793(01)03106-4

Cite this

@article{9b5aa96f8443415f93890054c0f97a41,

title = "Hydrogen peroxide is a regulator of ABI1, a protein phosphatase 2C from Arabidopsis",

abstract = "Protein phosphatases 2C (PP2Cs) exhibit diverse regulatory functions in signalling pathways of animals, yeast and plants. ABI1 is a PP2C of Arabidopsis that exerts negative control on signalling of the phytohormone abscisic acid (ABA). Characterisation of the redox sensitivity of ABI1 revealed a strong enzymatic inactivation by hydrogen peroxide (H2O2) which has recently been implicated as a secondary messenger of ABA signalling. H2O2 reversibly inhibited ABI1 activity in vitro with an IC50 of approximately 140 μM in the presence of physiological concentrations of glutathione. In addition, ABI1 was highly susceptible to inactivation by phenylarsine oxide (IC50=3-4 μM) indicative for the facile oxidation of vicinal cysteine residues. Thus, H2O2 generated during ABA signalling seems to inactivate the negative regulator of the ABA response.",

keywords = "Abscisic acid, Arabidopsis, Plant hormone, Protein phosphatase 2C, Signalling",

author = "Michael Meinhard and Erwin Grill",

note = "Funding Information: The financial support of the DFG and Fonds der Chemischen Industrie is gratefully acknowledged. ",

year = "2001",

month = nov,

day = "23",

doi = "10.1016/S0014-5793(01)03106-4",

language = "English",

volume = "508",

pages = "443--446",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "John Wiley and Sons Inc.",

number = "3",

}

TY - JOUR

T1 - Hydrogen peroxide is a regulator of ABI1, a protein phosphatase 2C from Arabidopsis

AU - Meinhard, Michael

AU - Grill, Erwin

N1 - Funding Information: The financial support of the DFG and Fonds der Chemischen Industrie is gratefully acknowledged.

PY - 2001/11/23

Y1 - 2001/11/23

N2 - Protein phosphatases 2C (PP2Cs) exhibit diverse regulatory functions in signalling pathways of animals, yeast and plants. ABI1 is a PP2C of Arabidopsis that exerts negative control on signalling of the phytohormone abscisic acid (ABA). Characterisation of the redox sensitivity of ABI1 revealed a strong enzymatic inactivation by hydrogen peroxide (H2O2) which has recently been implicated as a secondary messenger of ABA signalling. H2O2 reversibly inhibited ABI1 activity in vitro with an IC50 of approximately 140 μM in the presence of physiological concentrations of glutathione. In addition, ABI1 was highly susceptible to inactivation by phenylarsine oxide (IC50=3-4 μM) indicative for the facile oxidation of vicinal cysteine residues. Thus, H2O2 generated during ABA signalling seems to inactivate the negative regulator of the ABA response.

AB - Protein phosphatases 2C (PP2Cs) exhibit diverse regulatory functions in signalling pathways of animals, yeast and plants. ABI1 is a PP2C of Arabidopsis that exerts negative control on signalling of the phytohormone abscisic acid (ABA). Characterisation of the redox sensitivity of ABI1 revealed a strong enzymatic inactivation by hydrogen peroxide (H2O2) which has recently been implicated as a secondary messenger of ABA signalling. H2O2 reversibly inhibited ABI1 activity in vitro with an IC50 of approximately 140 μM in the presence of physiological concentrations of glutathione. In addition, ABI1 was highly susceptible to inactivation by phenylarsine oxide (IC50=3-4 μM) indicative for the facile oxidation of vicinal cysteine residues. Thus, H2O2 generated during ABA signalling seems to inactivate the negative regulator of the ABA response.

KW - Abscisic acid

KW - Arabidopsis

KW - Plant hormone

KW - Protein phosphatase 2C

KW - Signalling

UR - http://www.scopus.com/inward/record.url?scp=0035941064&partnerID=8YFLogxK

U2 - 10.1016/S0014-5793(01)03106-4

DO - 10.1016/S0014-5793(01)03106-4

M3 - Article

C2 - 11728469

AN - SCOPUS:0035941064

SN - 0014-5793

VL - 508

SP - 443

EP - 446

JO - FEBS Letters

JF - FEBS Letters

IS - 3

ER -

Hydrogen peroxide is a regulator of ABI1, a protein phosphatase 2C from Arabidopsis

Abstract

Keywords

Access to Document

Other files and links

Fingerprint

Cite this