Isolation and characterization of a 60 kDa 2,4-D-binding protein from the shoot apices of peach trees (Prunus persica L.);: It is a homologue of protein disulfide isomerase

被引：0

作者：

Sugaya, S ^{[1
]}

Ohmiya, A ^{[1
]}

Kikuchi, M ^{[1
]}

Hayashi, T ^{[1
]}

机构：

[1] Minist Agr Forestry & Fisheries, Natl Inst Fruit Tree Sci, Tsukuba, Ibaraki 3058605, Japan

来源：

PLANT AND CELL PHYSIOLOGY | 2000年 / 41卷 / 04期

关键词：

2,4-dichlorophenoxyacetic acid (2,4-D); protein disulfide isomerase (PDI) (EC 5.3.4.1); Prunus persica L-(peach);

D O I：

暂无

中图分类号：

Q94 [植物学];

学科分类号：

071001 ;

摘要：

To obtain a candidate auxin-binding protein (ABP), a soluble 60 kDa protein was isolated from an extract of shoot apices of peach trees (Prunus persica L.) by affinity chromatography on a 2,4-dichlorophenoxyacetic acid (2,4-D)-linked Sepharose4B column. The 60 kDa polypeptide, designated Pp60, was purified as a single band on SDS-PAGE by column chromatography. Its dissociation constant (Kd) for [C-14]-2,4-D was calculated to be 3.5 x 10(-5) M. The binding of Pp60 for [C-14]-2,4-D was inhibited by naphthalene-l-acetic acid (NAA) and p-chlorophenoxyiso-butyric acid (PCIB) as well as 2,4-D. Indole-3-acetic acid (IAA) had little effect on the binding. These results suggested that Pp60 is a protein that has an affinity for 2,4-D, NAA, and PCIB in vitro. The partial amino acid sequences of Pp60 showed high homology to those of protein disulfide isomerase (EC 5.3.4.1). Immunoblot analysis demonstrated that Pp60 exists ubiquitously in shoots and leaves. In fruit, expression of Pp60 is restricted at an early stage of development.

引用

页码：503 / 508

页数：6