AtVPS34, a phosphatidylinositol 3-kinase of Arabidopsis thaliana, is an essential protein with homology to a calcium-dependent lipid binding domain

Peter Welters, Kaoru Takegawa, Scott D. Emr, Maarten J. Chrispeels

研究成果: ジャーナルへの寄稿記事

139 引用 (Scopus)

抄録

The cDNA encoding phosphatidylinositol (PI) 3-kinase was cloned from Arabidopsis thaliana, and the derived amino acid sequence (AtVPS34) has a significantly higher homology to yeast PI 3-kinase (VPS34) than to the mammalian (p110). The protein has two conserved domains: a catalytic site with the ATP-binding site near the C terminus and a calcium-dependent lipid- binding domain near the N terminus. The plant cDNA does not rescue a yeast vps34 deletion mutant, but a chimeric gene in which the coding sequence for the C-terminal third of VPS34 is replaced by the corresponding sequence from the plant gene does rescue the yeast mutant. PI 3-kinase activity is detectable in extracts from plants that overexpress the plant PI 3-kinase. Expression of antisense constructs gives rise to second-generation transformed plants severely inhibited in growth and development.

元の言語英語
ページ(範囲)11398-11402
ページ数5
ジャーナルProceedings of the National Academy of Sciences of the United States of America
91
発行部数24
DOI
出版物ステータス出版済み - 11 22 1994

Fingerprint

Phosphatidylinositol 3-Kinase
Arabidopsis
Calcium
Lipids
Yeasts
Proteins
Complementary DNA
Plant Genes
Plant Extracts
Growth and Development
Amino Acid Sequence
Catalytic Domain
Adenosine Triphosphate
Binding Sites
Genes

All Science Journal Classification (ASJC) codes

  • General

これを引用

@article{67c997dc1ae34b1bb4b0d732ba8b0fc8,
title = "AtVPS34, a phosphatidylinositol 3-kinase of Arabidopsis thaliana, is an essential protein with homology to a calcium-dependent lipid binding domain",
abstract = "The cDNA encoding phosphatidylinositol (PI) 3-kinase was cloned from Arabidopsis thaliana, and the derived amino acid sequence (AtVPS34) has a significantly higher homology to yeast PI 3-kinase (VPS34) than to the mammalian (p110). The protein has two conserved domains: a catalytic site with the ATP-binding site near the C terminus and a calcium-dependent lipid- binding domain near the N terminus. The plant cDNA does not rescue a yeast vps34 deletion mutant, but a chimeric gene in which the coding sequence for the C-terminal third of VPS34 is replaced by the corresponding sequence from the plant gene does rescue the yeast mutant. PI 3-kinase activity is detectable in extracts from plants that overexpress the plant PI 3-kinase. Expression of antisense constructs gives rise to second-generation transformed plants severely inhibited in growth and development.",
author = "Peter Welters and Kaoru Takegawa and Emr, {Scott D.} and Chrispeels, {Maarten J.}",
year = "1994",
month = "11",
day = "22",
doi = "10.1073/pnas.91.24.11398",
language = "English",
volume = "91",
pages = "11398--11402",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
number = "24",

}

TY - JOUR

T1 - AtVPS34, a phosphatidylinositol 3-kinase of Arabidopsis thaliana, is an essential protein with homology to a calcium-dependent lipid binding domain

AU - Welters, Peter

AU - Takegawa, Kaoru

AU - Emr, Scott D.

AU - Chrispeels, Maarten J.

PY - 1994/11/22

Y1 - 1994/11/22

N2 - The cDNA encoding phosphatidylinositol (PI) 3-kinase was cloned from Arabidopsis thaliana, and the derived amino acid sequence (AtVPS34) has a significantly higher homology to yeast PI 3-kinase (VPS34) than to the mammalian (p110). The protein has two conserved domains: a catalytic site with the ATP-binding site near the C terminus and a calcium-dependent lipid- binding domain near the N terminus. The plant cDNA does not rescue a yeast vps34 deletion mutant, but a chimeric gene in which the coding sequence for the C-terminal third of VPS34 is replaced by the corresponding sequence from the plant gene does rescue the yeast mutant. PI 3-kinase activity is detectable in extracts from plants that overexpress the plant PI 3-kinase. Expression of antisense constructs gives rise to second-generation transformed plants severely inhibited in growth and development.

AB - The cDNA encoding phosphatidylinositol (PI) 3-kinase was cloned from Arabidopsis thaliana, and the derived amino acid sequence (AtVPS34) has a significantly higher homology to yeast PI 3-kinase (VPS34) than to the mammalian (p110). The protein has two conserved domains: a catalytic site with the ATP-binding site near the C terminus and a calcium-dependent lipid- binding domain near the N terminus. The plant cDNA does not rescue a yeast vps34 deletion mutant, but a chimeric gene in which the coding sequence for the C-terminal third of VPS34 is replaced by the corresponding sequence from the plant gene does rescue the yeast mutant. PI 3-kinase activity is detectable in extracts from plants that overexpress the plant PI 3-kinase. Expression of antisense constructs gives rise to second-generation transformed plants severely inhibited in growth and development.

UR - http://www.scopus.com/inward/record.url?scp=0027942615&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0027942615&partnerID=8YFLogxK

U2 - 10.1073/pnas.91.24.11398

DO - 10.1073/pnas.91.24.11398

M3 - Article

C2 - 7972072

AN - SCOPUS:0027942615

VL - 91

SP - 11398

EP - 11402

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

SN - 0027-8424

IS - 24

ER -