Functional comparisons between plant plasma membrane H+-ATPase isoforms expressed in yeast

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Functional comparisons between plant plasma membrane H+-ATPase isoforms expressed in yeast. / Palmgren, Michael Gjedde; Christensen, Gertrud.

In: Journal of Biological Chemistry, Vol. 269, No. 4, 28.01.1994, p. 3027-3033.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Palmgren, MG & Christensen, G 1994, 'Functional comparisons between plant plasma membrane H+-ATPase isoforms expressed in yeast', Journal of Biological Chemistry, vol. 269, no. 4, pp. 3027-3033.

APA

Palmgren, M. G., & Christensen, G. (1994). Functional comparisons between plant plasma membrane H+-ATPase isoforms expressed in yeast. Journal of Biological Chemistry, 269(4), 3027-3033.

Vancouver

Palmgren MG, Christensen G. Functional comparisons between plant plasma membrane H+-ATPase isoforms expressed in yeast. Journal of Biological Chemistry. 1994 Jan 28;269(4):3027-3033.

Author

Palmgren, Michael Gjedde ; Christensen, Gertrud. / Functional comparisons between plant plasma membrane H+-ATPase isoforms expressed in yeast. In: Journal of Biological Chemistry. 1994 ; Vol. 269, No. 4. pp. 3027-3033.

Bibtex

@article{ba0f64659544472b8a7fc0c6740d9ce9,
title = "Functional comparisons between plant plasma membrane H+-ATPase isoforms expressed in yeast",
abstract = "To examine the functional properties of the three major isoforms of plasma membrane H+-ATPase expressed in Arabidopsis thaliana (AHA1, AHA2, and AHA3), we employed a system for the heterologous expression of functional plant plasma membrane H+-ATPase in yeast (Villalba, J. M., Palmgren, M. G., Berberian, G. E., Ferguson, C., and Serrano, R. (1992) J. Biol. Chem. 267, 12341-12349). Each isoform was expressed efficiently but appeared to be retained in the endoplasmic reticulum of yeast. All isoforms displayed qualitatively similar enzymatic properties, but quantitative differences were found. When compared with AHA3, AHA1 and AHA2 had an apparent higher turnover rate for ATP hydrolysis, exhibited a 10-fold higher apparent affinity for ATP, and a 3-fold higher sensitivity toward vanadate. In addition, AHA2 had a slightly lower apparent affinity for H+ and seemed to be more susceptible to activation by lysophosphatidylcholine than did AHA1 and AHA3. This study represents the first comparison of the functional properties of isoforms of the plant plasma membrane H+-ATPase.",
author = "Palmgren, {Michael Gjedde} and Gertrud Christensen",
year = "1994",
month = jan,
day = "28",
language = "English",
volume = "269",
pages = "3027--3033",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",
number = "4",

}

RIS

TY - JOUR

T1 - Functional comparisons between plant plasma membrane H+-ATPase isoforms expressed in yeast

AU - Palmgren, Michael Gjedde

AU - Christensen, Gertrud

PY - 1994/1/28

Y1 - 1994/1/28

N2 - To examine the functional properties of the three major isoforms of plasma membrane H+-ATPase expressed in Arabidopsis thaliana (AHA1, AHA2, and AHA3), we employed a system for the heterologous expression of functional plant plasma membrane H+-ATPase in yeast (Villalba, J. M., Palmgren, M. G., Berberian, G. E., Ferguson, C., and Serrano, R. (1992) J. Biol. Chem. 267, 12341-12349). Each isoform was expressed efficiently but appeared to be retained in the endoplasmic reticulum of yeast. All isoforms displayed qualitatively similar enzymatic properties, but quantitative differences were found. When compared with AHA3, AHA1 and AHA2 had an apparent higher turnover rate for ATP hydrolysis, exhibited a 10-fold higher apparent affinity for ATP, and a 3-fold higher sensitivity toward vanadate. In addition, AHA2 had a slightly lower apparent affinity for H+ and seemed to be more susceptible to activation by lysophosphatidylcholine than did AHA1 and AHA3. This study represents the first comparison of the functional properties of isoforms of the plant plasma membrane H+-ATPase.

AB - To examine the functional properties of the three major isoforms of plasma membrane H+-ATPase expressed in Arabidopsis thaliana (AHA1, AHA2, and AHA3), we employed a system for the heterologous expression of functional plant plasma membrane H+-ATPase in yeast (Villalba, J. M., Palmgren, M. G., Berberian, G. E., Ferguson, C., and Serrano, R. (1992) J. Biol. Chem. 267, 12341-12349). Each isoform was expressed efficiently but appeared to be retained in the endoplasmic reticulum of yeast. All isoforms displayed qualitatively similar enzymatic properties, but quantitative differences were found. When compared with AHA3, AHA1 and AHA2 had an apparent higher turnover rate for ATP hydrolysis, exhibited a 10-fold higher apparent affinity for ATP, and a 3-fold higher sensitivity toward vanadate. In addition, AHA2 had a slightly lower apparent affinity for H+ and seemed to be more susceptible to activation by lysophosphatidylcholine than did AHA1 and AHA3. This study represents the first comparison of the functional properties of isoforms of the plant plasma membrane H+-ATPase.

UR - http://www.scopus.com/inward/record.url?scp=0028070772&partnerID=8YFLogxK

M3 - Journal article

C2 - 8300635

AN - SCOPUS:0028070772

VL - 269

SP - 3027

EP - 3033

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 4

ER -

ID: 245002993