Journal Article

Isolation and Characterization of a 60 kDa 2,4-D-Binding Protein from the Shoot Apices of Peach Trees (<i>Prunus persica</i> L.); It Is a Homologue of Protein Disulfide Isomerase

Sumiko Sugaya, Akemi Ohmiya, Motoyuki Kikuchi and Tateki Hayashi

in Plant and Cell Physiology

Published on behalf of Japanese Society of Plant Physiologists

Volume 41, issue 4, pages 503-508
Published in print April 2000 | ISSN: 0032-0781
Published online April 2000 | e-ISSN: 1471-9053 | DOI: http://dx.doi.org/10.1093/pcp/41.4.503
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

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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 [14C]-2,4-D was calculated to be 3.5 × 10−5 M. The binding of Pp60 for [14C]-2,4-D was inhibited by naphthalene-1-acetic acid (NAA) and p-chlorophenoxyisobutyric 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.

Keywords: 2,4-Dichlorophenoxyacetic acid (2,4-D); Protein disulfide isomerase (PDI) (EC 5.3.4.1); Prunus persica L. (peach)

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Subjects: Biochemistry ; Molecular and Cell Biology ; Plant Sciences and Forestry

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