The regulatory domain of fungal and plant plasma membrane H+-ATPase

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The regulatory domain of fungal and plant plasma membrane H+-ATPase. / Serrano, R.; Portillo, F.; Monk, B. C.; Palmgren, M. G.

In: Acta Physiologica Scandinavica, Supplement, Vol. 146, No. 607, 1992, p. 131-136.

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

Harvard

Serrano, R, Portillo, F, Monk, BC & Palmgren, MG 1992, 'The regulatory domain of fungal and plant plasma membrane H+-ATPase', Acta Physiologica Scandinavica, Supplement, vol. 146, no. 607, pp. 131-136.

APA

Serrano, R., Portillo, F., Monk, B. C., & Palmgren, M. G. (1992). The regulatory domain of fungal and plant plasma membrane H+-ATPase. Acta Physiologica Scandinavica, Supplement, 146(607), 131-136.

Vancouver

Serrano R, Portillo F, Monk BC, Palmgren MG. The regulatory domain of fungal and plant plasma membrane H+-ATPase. Acta Physiologica Scandinavica, Supplement. 1992;146(607):131-136.

Author

Serrano, R. ; Portillo, F. ; Monk, B. C. ; Palmgren, M. G. / The regulatory domain of fungal and plant plasma membrane H+-ATPase. In: Acta Physiologica Scandinavica, Supplement. 1992 ; Vol. 146, No. 607. pp. 131-136.

Bibtex

@article{b97c8840a825477caaf88f9ef221a7e8,
title = "The regulatory domain of fungal and plant plasma membrane H+-ATPase",
abstract = "The activity of fungal and plant plasma membrane H+-ATPases seems to be regulated by modulation of the interaction of an inhibitory domain at the C-terminus with the active site. In the yeast ATPase, a mutation at the active site (Ala547- > Val) and a deletion of the C-terminus result in constitutive activation. A double Ser911- > Ala, Thr912- > Ala mutation at the C-terminus (defining putative phosphorylation sites) locks the enzyme in the inhibited state and can be suppressed by the Ala547- > Val mutation at the active site. This provides genetic evidence for domain interaction. In plant ATPase, proteolytic removal of the C-terminus also results in constitutive activation. A peptide covering a region of the plant C-terminus with homology to the yeast C-terminus inhibits the truncated plant ATPase. This suggests similar regulatory mechanisms in fungal and plant ATPases.",
author = "R. Serrano and F. Portillo and Monk, {B. C.} and Palmgren, {M. G.}",
year = "1992",
language = "English",
volume = "146",
pages = "131--136",
journal = "Acta Physiologica Scandinavica",
issn = "0001-6772",
publisher = "Blackwell Science Ltd.",
number = "607",

}

RIS

TY - JOUR

T1 - The regulatory domain of fungal and plant plasma membrane H+-ATPase

AU - Serrano, R.

AU - Portillo, F.

AU - Monk, B. C.

AU - Palmgren, M. G.

PY - 1992

Y1 - 1992

N2 - The activity of fungal and plant plasma membrane H+-ATPases seems to be regulated by modulation of the interaction of an inhibitory domain at the C-terminus with the active site. In the yeast ATPase, a mutation at the active site (Ala547- > Val) and a deletion of the C-terminus result in constitutive activation. A double Ser911- > Ala, Thr912- > Ala mutation at the C-terminus (defining putative phosphorylation sites) locks the enzyme in the inhibited state and can be suppressed by the Ala547- > Val mutation at the active site. This provides genetic evidence for domain interaction. In plant ATPase, proteolytic removal of the C-terminus also results in constitutive activation. A peptide covering a region of the plant C-terminus with homology to the yeast C-terminus inhibits the truncated plant ATPase. This suggests similar regulatory mechanisms in fungal and plant ATPases.

AB - The activity of fungal and plant plasma membrane H+-ATPases seems to be regulated by modulation of the interaction of an inhibitory domain at the C-terminus with the active site. In the yeast ATPase, a mutation at the active site (Ala547- > Val) and a deletion of the C-terminus result in constitutive activation. A double Ser911- > Ala, Thr912- > Ala mutation at the C-terminus (defining putative phosphorylation sites) locks the enzyme in the inhibited state and can be suppressed by the Ala547- > Val mutation at the active site. This provides genetic evidence for domain interaction. In plant ATPase, proteolytic removal of the C-terminus also results in constitutive activation. A peptide covering a region of the plant C-terminus with homology to the yeast C-terminus inhibits the truncated plant ATPase. This suggests similar regulatory mechanisms in fungal and plant ATPases.

UR - http://www.scopus.com/inward/record.url?scp=0026620754&partnerID=8YFLogxK

M3 - Journal article

C2 - 1449059

AN - SCOPUS:0026620754

VL - 146

SP - 131

EP - 136

JO - Acta Physiologica Scandinavica

JF - Acta Physiologica Scandinavica

SN - 0001-6772

IS - 607

ER -

ID: 245002215