The photoconvertible water-soluble chlorophyll-binding protein of Chenopodium album is a member of DUF538, a superfamily that distributes in Embryophyta

The photoconvertible water-soluble chlorophyll-binding protein of Chenopodium album is a member of DUF538, a superfamily that distributes in Embryophyta

Copyright © 2013 Elsevier GmbH. All rights reserved.

Bibliographische Detailangaben
Veröffentlicht in:Journal of plant physiology. - 1979. - 170(2013), 17 vom: 15. Nov., Seite 1549-52
1. Verfasser: Takahashi, Shigekazu (VerfasserIn)
Weitere Verfasser: Yoshikawa, Mami, Kamada, Akiko, Ohtsuki, Takayuki, Uchida, Akira, Nakayama, Katsumi, Satoh, Hiroyuki
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2013
Zugriff auf das übergeordnete Werk:Journal of plant physiology
Schlagworte:Journal Article C-terminal Chenopodium album Chl Chlorophyll DUF DUF538 IPTG N-terminal Photoconversion mehr... WSCP Water-soluble chlorophyll-binding protein amino terminal carboxy terminal chlorophyll domain of unknown function isopropyl β-d-1-thiogalactopyranoside water-soluble chlorophyll-binding protein Chlorophyll Binding Proteins
Beschreibung
Zusammenfassung:Copyright © 2013 Elsevier GmbH. All rights reserved.
Various plants possess hydrophilic chlorophyll (Chl) proteins known as water-soluble Chl-binding proteins (WSCPs). WSCPs exist in two forms: Class I and Class II, of which Class I alone exhibits unique photoconvertibility. Although numerous genes encoding Class II WSCPs have been identified and the molecular properties of their recombinant proteins have been well characterized, no Class I WSCP gene has been identified to date. In this study, we cloned the cDNA and a gene encoding the Class I WSCP of Chenopodium album (CaWSCP). Sequence analyses revealed that CaWSCP comprises a single exon corresponding to 585bp of an open reading frame encoding 195 amino acid residues. The CaWSCP protein sequence possesses a signature of DUF538, a protein superfamily of unknown function found almost exclusively in Embryophyta. The recombinant CaWSCP was expressed in Escherichia coli as a hexa-histidine fusion protein (CaWSCP-His) that removes Chls from the thylakoid. Under visible light illumination, the reconstituted CaWSCP-His was successfully photoconverted into a different pigment with an absorption spectrum identical to that of native CaWSCP. Interestingly, while CaWSCP-His could bind both Chl a and Chl b, photoconversion occurred only in CaWSCP-His reconstituted with Chl a
Beschreibung:Date Completed 09.06.2014
Date Revised 30.09.2020
published: Print-Electronic
Citation Status MEDLINE
ISSN:1618-1328
DOI:10.1016/j.jplph.2013.06.001