Characterization of Arabidopsis secretory phospholipase A 2-γ cDNA and its enzymatic properties

Sung Chul Bahn; Hyoung Yool Lee; Hae Jin Kim; Stephen B. Ryu; Jeong Sheop Shin

doi:10.1016/S0014-5793(03)00982-7

Characterization of Arabidopsis secretory phospholipase A ₂-γ cDNA and its enzymatic properties

Sung Chul Bahn, Hyoung Yool Lee, Hae Jin Kim, Stephen B. Ryu, Jeong Sheop Shin

Division of life Sciences

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

30 Citations (Scopus)

Abstract

Plant secretory phospholipases A₂ (sPLA₂s) probably play important roles in phospholipid signaling based on the data reported from other organisms, but their functions are poorly understood because of the lack of cloned sPLA₂ genes. In this study, we cloned and characterized an Arabidopsis secretory phospholipase A₂-γ (AtsPLA ₂-γ) cDNA, and examined its enzymatic properties. The recombinant protein of AtsPLA₂-γ showed maximal enzyme activity at pH 8.0, and required Ca²⁺ for activity. Moreover, AtsPLA₂-γ showed sn-2 position specificity but no prominent acyl preference, though it showed head group specificity to phosphatidylethanolamine rather than to phosphatidylcholine. AtsPLA ₂-γ was found to predominate in the mature flower rather than in other tissues, and subcellular localization analysis confirmed that AtsPLA₂-γ is secreted into the intercellular space.

Original language	English
Pages (from-to)	113-118
Number of pages	6
Journal	FEBS Letters
Volume	553
Issue number	1-2
DOIs	https://doi.org/10.1016/S0014-5793(03)00982-7
Publication status	Published - 2003 Oct 9

Keywords

AtsPLA-γ
Lysophospholipid
Phosphatidylcholine
Phosphatidylethanolamine
Phospholipid
Secretory phospholipase A

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

Access to Document

10.1016/S0014-5793(03)00982-7

Cite this

@article{fa75d48cb2ea46c1a58a740bc14c6b96,

title = "Characterization of Arabidopsis secretory phospholipase A 2-γ cDNA and its enzymatic properties",

abstract = "Plant secretory phospholipases A2 (sPLA2s) probably play important roles in phospholipid signaling based on the data reported from other organisms, but their functions are poorly understood because of the lack of cloned sPLA2 genes. In this study, we cloned and characterized an Arabidopsis secretory phospholipase A2-γ (AtsPLA 2-γ) cDNA, and examined its enzymatic properties. The recombinant protein of AtsPLA2-γ showed maximal enzyme activity at pH 8.0, and required Ca2+ for activity. Moreover, AtsPLA2-γ showed sn-2 position specificity but no prominent acyl preference, though it showed head group specificity to phosphatidylethanolamine rather than to phosphatidylcholine. AtsPLA 2-γ was found to predominate in the mature flower rather than in other tissues, and subcellular localization analysis confirmed that AtsPLA2-γ is secreted into the intercellular space.",

keywords = "AtsPLA-γ, Lysophospholipid, Phosphatidylcholine, Phosphatidylethanolamine, Phospholipid, Secretory phospholipase A",

author = "Bahn, {Sung Chul} and Lee, {Hyoung Yool} and Kim, {Hae Jin} and Ryu, {Stephen B.} and Shin, {Jeong Sheop}",

note = "Funding Information: This project was funded by a grant (to J.S.S.) from the Crop Functional Genomics Center of the 21st Century Frontier Research Program and a grant (to S.B.R.) from the Plant Diversity Research Center of the 21st Century Frontier Research Program funded by the Ministry of Science and Technology of the Korean government.",

year = "2003",

month = oct,

day = "9",

doi = "10.1016/S0014-5793(03)00982-7",

language = "English",

volume = "553",

pages = "113--118",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "Elsevier",

number = "1-2",

}

TY - JOUR

T1 - Characterization of Arabidopsis secretory phospholipase A 2-γ cDNA and its enzymatic properties

AU - Bahn, Sung Chul

AU - Lee, Hyoung Yool

AU - Kim, Hae Jin

AU - Ryu, Stephen B.

AU - Shin, Jeong Sheop

N1 - Funding Information: This project was funded by a grant (to J.S.S.) from the Crop Functional Genomics Center of the 21st Century Frontier Research Program and a grant (to S.B.R.) from the Plant Diversity Research Center of the 21st Century Frontier Research Program funded by the Ministry of Science and Technology of the Korean government.

PY - 2003/10/9

Y1 - 2003/10/9

N2 - Plant secretory phospholipases A2 (sPLA2s) probably play important roles in phospholipid signaling based on the data reported from other organisms, but their functions are poorly understood because of the lack of cloned sPLA2 genes. In this study, we cloned and characterized an Arabidopsis secretory phospholipase A2-γ (AtsPLA 2-γ) cDNA, and examined its enzymatic properties. The recombinant protein of AtsPLA2-γ showed maximal enzyme activity at pH 8.0, and required Ca2+ for activity. Moreover, AtsPLA2-γ showed sn-2 position specificity but no prominent acyl preference, though it showed head group specificity to phosphatidylethanolamine rather than to phosphatidylcholine. AtsPLA 2-γ was found to predominate in the mature flower rather than in other tissues, and subcellular localization analysis confirmed that AtsPLA2-γ is secreted into the intercellular space.

AB - Plant secretory phospholipases A2 (sPLA2s) probably play important roles in phospholipid signaling based on the data reported from other organisms, but their functions are poorly understood because of the lack of cloned sPLA2 genes. In this study, we cloned and characterized an Arabidopsis secretory phospholipase A2-γ (AtsPLA 2-γ) cDNA, and examined its enzymatic properties. The recombinant protein of AtsPLA2-γ showed maximal enzyme activity at pH 8.0, and required Ca2+ for activity. Moreover, AtsPLA2-γ showed sn-2 position specificity but no prominent acyl preference, though it showed head group specificity to phosphatidylethanolamine rather than to phosphatidylcholine. AtsPLA 2-γ was found to predominate in the mature flower rather than in other tissues, and subcellular localization analysis confirmed that AtsPLA2-γ is secreted into the intercellular space.

KW - AtsPLA-γ

KW - Lysophospholipid

KW - Phosphatidylcholine

KW - Phosphatidylethanolamine

KW - Phospholipid

KW - Secretory phospholipase A

UR - http://www.scopus.com/inward/record.url?scp=0141459685&partnerID=8YFLogxK

U2 - 10.1016/S0014-5793(03)00982-7

DO - 10.1016/S0014-5793(03)00982-7

M3 - Article

C2 - 14550557

AN - SCOPUS:0141459685

SN - 0014-5793

VL - 553

SP - 113

EP - 118

JO - FEBS Letters

JF - FEBS Letters

IS - 1-2

ER -