|
|
|
|
| LEADER |
01000caa a22002652 4500 |
| 001 |
NLM228843030 |
| 003 |
DE-627 |
| 005 |
20250215144653.0 |
| 007 |
cr uuu---uuuuu |
| 008 |
231224s2013 xx |||||o 00| ||eng c |
| 024 |
7 |
|
|a 10.1016/j.jplph.2013.06.001
|2 doi
|
| 028 |
5 |
2 |
|a pubmed25n0762.xml
|
| 035 |
|
|
|a (DE-627)NLM228843030
|
| 035 |
|
|
|a (NLM)23820553
|
| 035 |
|
|
|a (PII)S0176-1617(13)00241-1
|
| 040 |
|
|
|a DE-627
|b ger
|c DE-627
|e rakwb
|
| 041 |
|
|
|a eng
|
| 100 |
1 |
|
|a Takahashi, Shigekazu
|e verfasserin
|4 aut
|
| 245 |
1 |
4 |
|a The photoconvertible water-soluble chlorophyll-binding protein of Chenopodium album is a member of DUF538, a superfamily that distributes in Embryophyta
|
| 264 |
|
1 |
|c 2013
|
| 336 |
|
|
|a Text
|b txt
|2 rdacontent
|
| 337 |
|
|
|a ƒaComputermedien
|b c
|2 rdamedia
|
| 338 |
|
|
|a ƒa Online-Ressource
|b cr
|2 rdacarrier
|
| 500 |
|
|
|a Date Completed 09.06.2014
|
| 500 |
|
|
|a Date Revised 30.09.2020
|
| 500 |
|
|
|a published: Print-Electronic
|
| 500 |
|
|
|a Citation Status MEDLINE
|
| 520 |
|
|
|a Copyright © 2013 Elsevier GmbH. All rights reserved.
|
| 520 |
|
|
|a 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
|
| 650 |
|
4 |
|a Journal Article
|
| 650 |
|
4 |
|a C-terminal
|
| 650 |
|
4 |
|a Chenopodium album
|
| 650 |
|
4 |
|a Chl
|
| 650 |
|
4 |
|a Chlorophyll
|
| 650 |
|
4 |
|a DUF
|
| 650 |
|
4 |
|a DUF538
|
| 650 |
|
4 |
|a IPTG
|
| 650 |
|
4 |
|a N-terminal
|
| 650 |
|
4 |
|a Photoconversion
|
| 650 |
|
4 |
|a WSCP
|
| 650 |
|
4 |
|a Water-soluble chlorophyll-binding protein
|
| 650 |
|
4 |
|a amino terminal
|
| 650 |
|
4 |
|a carboxy terminal
|
| 650 |
|
4 |
|a chlorophyll
|
| 650 |
|
4 |
|a domain of unknown function
|
| 650 |
|
4 |
|a isopropyl β-d-1-thiogalactopyranoside
|
| 650 |
|
4 |
|a water-soluble chlorophyll-binding protein
|
| 650 |
|
7 |
|a Chlorophyll Binding Proteins
|2 NLM
|
| 700 |
1 |
|
|a Yoshikawa, Mami
|e verfasserin
|4 aut
|
| 700 |
1 |
|
|a Kamada, Akiko
|e verfasserin
|4 aut
|
| 700 |
1 |
|
|a Ohtsuki, Takayuki
|e verfasserin
|4 aut
|
| 700 |
1 |
|
|a Uchida, Akira
|e verfasserin
|4 aut
|
| 700 |
1 |
|
|a Nakayama, Katsumi
|e verfasserin
|4 aut
|
| 700 |
1 |
|
|a Satoh, Hiroyuki
|e verfasserin
|4 aut
|
| 773 |
0 |
8 |
|i Enthalten in
|t Journal of plant physiology
|d 1979
|g 170(2013), 17 vom: 15. Nov., Seite 1549-52
|w (DE-627)NLM098174622
|x 1618-1328
|7 nnns
|
| 773 |
1 |
8 |
|g volume:170
|g year:2013
|g number:17
|g day:15
|g month:11
|g pages:1549-52
|
| 856 |
4 |
0 |
|u http://dx.doi.org/10.1016/j.jplph.2013.06.001
|3 Volltext
|
| 912 |
|
|
|a GBV_USEFLAG_A
|
| 912 |
|
|
|a SYSFLAG_A
|
| 912 |
|
|
|a GBV_NLM
|
| 912 |
|
|
|a GBV_ILN_350
|
| 951 |
|
|
|a AR
|
| 952 |
|
|
|d 170
|j 2013
|e 17
|b 15
|c 11
|h 1549-52
|