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

Takahashi, Shingo; Yoshikawa, Mami; Kamada, Akiko; Ohtsuki, Tsuyuka; Uchida, Akira; Nakayama, Katsumi; Satoh, Hiroyuki

doi:10.1016/j.jplph.2013.06.001

Cited by 21 publications

(44 citation statements)

References 24 publications

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“…CaWSCP possesses an N-terminal extension predicted to be a signal peptide and a C-terminal extension whose function has not been characterized. 33) CfWSCP1 and CfWSCP2 also possess these extensions. Furthermore, the cysteine residues corresponding to cystein2 and cystein30 that are essential for Chlbinding of CaWSCP 34) are conserved in CfWSCP1 and CfWSCP2.…”

Section: Cloning Genes Encoding Cfwscpsmentioning

confidence: 97%

“…DUF538 superfamily members are distributed in Embryophyta. 33) In Arabidopsis thaliana, there are 22 genes encoding DUF538 proteins. 34) A phylogenetic tree of CaWSCP, CfWSCP1, CfWSCP2, and AtDUF538s is shown in Figure S2.…”

Section: Cloning Genes Encoding Cfwscpsmentioning

confidence: 99%

“…Similar to CaWSCP-His, 33) almost all CfWSCP1-His and CfWSCP2-His expressed in E. coli BL21 (DE3) were present in the insoluble fraction Notes: The alignment was generated by ClustalX. Black and gray arrows are post-translational cleavage sites for the signal peptide and C-terminal extension peptide, respectively.…”

Section: Cloning Genes Encoding Cfwscpsmentioning

confidence: 99%

“…33) To examine the photoconvertibilities of CfWSCP1-His and CfWSCP2-His reconstituted with Chl a or Chl b, we attempted to reconstitute CfWSCPs with purified Chl a or Chl b in a buffer containing 10% methanol. We obtained CfWSCP1-His reconstituted with Chl a or Chl b.…”

Section: Reconstitution and Photoconversion Of Cfwscp1-his And Cfwscpmentioning

confidence: 99%

“…18,[20][21][22][23][24][25][26][27][28][29][30][31][32] On the other hand, CaWSCP is the only gene encoding a Class I WSCP identified to date and few studies on the molecular genetics of the protein have been performed thus far. 33,34) Identification of novel genes encoding Class I WSCPs is essential for understanding the molecular diversity of the protein. In this study, we cloned two Chenopodium ficifolium genes encoding Class I WSCPs and expressed them in Escherichia coli to produce functional recombinant proteins.…”

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confidence: 99%

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Identification of genes encoding photoconvertible (Class I) water-soluble chlorophyll-binding proteins from Chenopodium ficifolium

Takahashi

Abe

Nakayama

et al. 2015

Bioscience, Biotechnology, and Biochemistry

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Photoconvertible water-soluble chlorophyll-binding proteins, called Class I WSCPs, have been detected in Chenopodiaceae, Amaranthaceae and Polygonaceae plant species. To date, Chenopodium album WSCP (CaWSCP) is the only cloned gene encoding a Class I WSCP. In this study, we identified two cDNAs encoding Chenopodium ficifolium Class I WSCPs, CfWSCP1, and CfWSCP2. Sequence analyses revealed that the open reading frames of CfWSCP1 and CfWSCP2 were 585 and 588 bp, respectively. Furthermore, both CfWSCPs contain cystein2 and cystein30, which are essential for the chlorophyll-binding ability of CaWSCP. Recombinant CfWSCP1 and CfWSCP2, expressed in Escherichia coli as hexa-histidine fusion proteins (CfWSCP1-His and CfWSCP2-His), formed inclusion bodies; however, we were able to solubilize these using a buffer containing 8 M urea and then refold them by dialysis. The refolded CfWSCP1-His and CfWSCP2-His could bind chlorophylls and exhibited photoconvertibility, confirming that the cloned CfWSCPs are further examples of Class I WSCPs.

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Section: Cloning Genes Encoding Cfwscpsmentioning

confidence: 97%

Section: Cloning Genes Encoding Cfwscpsmentioning

confidence: 99%

Section: Cloning Genes Encoding Cfwscpsmentioning

confidence: 99%

Section: Reconstitution and Photoconversion Of Cfwscp1-his And Cfwscpmentioning

confidence: 99%

mentioning

confidence: 99%

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Identification of genes encoding photoconvertible (Class I) water-soluble chlorophyll-binding proteins from Chenopodium ficifolium

Takahashi

Abe

Nakayama

et al. 2015

Bioscience, Biotechnology, and Biochemistry

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Genome-wide association mapping combined with gene-based haplotype analysis identify a novel gene for shoot length in rice (Oryza sativa L.)

Yang,

Dong,

Zhao

et al. 2023

Theor Appl Genet

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Key message Genome-wide association mapping revealed a novel QTL for shoot length across multiple environments. Its causal gene, LOC_Os01g68500, was identified firstly through gene-based haplotype analysis, gene expression and knockout transgenic verification. Abstract Strong seedling vigor is an important breeding target for rice varieties used in direct seeding. Shoot length (SL) is one of the important traits associated with seedling vigor characterized by rapid growth of seedling, which enhance seedling emergence. Therefore, mining genes for SL and conducting molecular breeding help to develop varieties for direct seeding. However, few QTLs for SL have been fine mapped or cloned so far. In this study, a genome-wide association study of SL was performed in a diverse rice collection consisting of 391 accessions in two years, using phenotypes generated by different cultivation methods according to the production practice, and a total of twenty-four QTLs for SL were identified. Among them, the novel QTL qSL-1f on chromosome 1 could be stably detected across all three cultivation methods in the whole population and indica subpopulation. Through gene-based haplotype analysis of the annotated genes within the putative region of qSL-1f, and validated by gene expression and knockout transgenic experiments, LOC_Os01g68500 (i.e., Os01g0913100 in RAP-DB) was identified as the causal gene for SL, which has a single-base variation (C-to-A transversion) in its CDS region, resulting in the significant difference in SL of rice. LOC_Os01g68500 encodes a DUF538 (Domain of unknown function) containing protein, and the function of DUF538 protein gene on rice seedling growth is firstly reported in this study. These results provide a new clue for exploring the molecular mechanism regulating SL, and promising gene source for the molecular breeding in rice.

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Molecular cloning, characterization and analysis of the intracellular localization of a water-soluble chlorophyll-binding protein (WSCP) from Virginia pepperweed (Lepidium virginicum), a unique WSCP that preferentially binds chlorophyll b in vitro

Takahashi

Yanai

Oka-Takayama

et al. 2013

Planta

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Various plants possess non-photosynthetic, hydrophilic chlorophyll (Chl) proteins called water-soluble Chl-binding proteins (WSCPs). WSCPs are categorized into two classes; Class I (photoconvertible type) and Class II (non-photoconvertible type). Among Class II WSCPs, only Lepidium virginicum WSCP (LvWSCP) exhibits a low Chl a/b ratio compared with that found in the leaf. Although the physicochemical properties of LvWSCP have been characterized, its molecular properties have not yet been documented. Here, we report the characteristics of the LvWSCP gene, the biochemical properties of a recombinant LvWSCP, and the intracellular localization of LvWSCP. The cloned LvWSCP gene possesses a 669-bp open reading frame. Matrix-assisted laser desorption ionization time-of-flight mass spectrometry analysis revealed that the precursor of LvWSCP contains both N- and C-terminal extension peptides. RT-PCR analysis revealed that LvWSCP was transcribed in various tissues, with the levels being higher in developing tissues. A recombinant LvWSCP and hexa-histidine fusion protein (LvWSCP-His) could remove Chls from the thylakoid in aqueous solution and showed an absorption spectrum identical to that of native LvWSCP. Although LvWSCP-His could bind both Chl a and Chl b, it bound almost exclusively to Chl b when reconstituted in 40 % methanol. To clarify the intracellular targeting functions of the N- and C-terminal extension peptides, we constructed transgenic Arabidopsis thaliana lines expressing the Venus protein fused with the LvWSCP N- and/or C-terminal peptides, as well as Venus fused at the C-terminus of LvWSCP. The results showed that the N-terminal peptide functioned in ER body targeting, while the C-terminal sequence did not act as a trailer peptide.

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

Cited by 21 publications

References 24 publications

Identification of genes encoding photoconvertible (Class I) water-soluble chlorophyll-binding proteins from Chenopodium ficifolium

Identification of genes encoding photoconvertible (Class I) water-soluble chlorophyll-binding proteins from Chenopodium ficifolium

Genome-wide association mapping combined with gene-based haplotype analysis identify a novel gene for shoot length in rice (Oryza sativa L.)

Molecular cloning, characterization and analysis of the intracellular localization of a water-soluble chlorophyll-binding protein (WSCP) from Virginia pepperweed (Lepidium virginicum), a unique WSCP that preferentially binds chlorophyll b in vitro

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