Cloned (Comment) | Organism |
---|---|
gene CsHY2, genotyping, several segregating populations qre employed by crossing C1238 with the original parental line CCMC, the American pickling cucumber line Gy14 and the North China fresh marker type cucumber line 9930, respectively. For linkage mapping and cloning of the elh1 gene, F2 populations are derived from the C1238×9930 F1 and C1238×Gy14 F1 plants, respectively. Quantitative real-time PCR enzyme expression analysis. Phylogenetic analysis of CsHY2 homologues from different plants. Linkage mapping of the elh1 locus | Cucumis sativus |
Protein Variants | Comment | Organism |
---|---|---|
additional information | identification of elongated hypocotyl-1 (elh1) mutant C1238, comparison of mutant seedlings with wild-type CCMC seedlings, phenotype, overview. Analysis of the effect of CsHY2 mutation on the function of phys, the expression dynamics of cucumber PHYs genes (CsPHYA1, CsPHYA2, CsPHYB, CsPHYC, and CsPHYE). The 35S:CsHY2-EGFP plasmid construct is transformed into Agrobacterium tumefaciens strain GV3101. Arabidopsis hy2-1 recessive homozygous mutants are transformed and the phenotype is analyzed. The expression level of CsHY2 in mutant is the highest in male and female flowers, followed in order by stem, true leaves, root, cotyledon, and fruit. There is no significant difference in CsHY2 expression in all these organs except cotyledons, true leaves, and stem between wild-type and mutant elh1 | Cucumis sativus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
chloroplast | the CsHY2 protein sequence contains an N-terminal chloroplast transit peptide (cTP) | Cucumis sativus | 9507 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | in cofactor ferrdoxin | Cucumis sativus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
biliverdin IXalpha + 2 reduced ferredoxin | Cucumis sativus | - |
(3Z)-phytochromobilin + 2 oxidized ferredoxin | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Cucumis sativus | A0A0A0LXG3 | - |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
hypocotyl | - |
Cucumis sativus | - |
additional information | spatiotemporal expression patterns of CsHY2 | Cucumis sativus | - |
seedling | - |
Cucumis sativus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
biliverdin IXalpha + 2 reduced ferredoxin | - |
Cucumis sativus | (3Z)-phytochromobilin + 2 oxidized ferredoxin | - |
? |
Synonyms | Comment | Organism |
---|---|---|
Csa_1G616870 | - |
Cucumis sativus |
CsHY2 | - |
Cucumis sativus |
HY2 protein | - |
Cucumis sativus |
phytochromobilin synthase | - |
Cucumis sativus |
PphiB synthase | - |
Cucumis sativus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
Ferredoxin | - |
Cucumis sativus |
General Information | Comment | Organism |
---|---|---|
evolution | phylogenetic analysis of CsHY2 homologues from different plants | Cucumis sativus |
malfunction | the long hypocotyl mutant C1238 is identified from an EMS-induced mutagenesis population of the cucumber inbred line CCMC with normal hypocotyl and green leaves. The mutant C1238 exhibits apparently elongated hypocotyl and yellow-green leaves at the seedling stage | Cucumis sativus |
physiological function | the CsHY2 protein plays a role in the chloroplast, which is consistent with the plastid localization of PPhiB synthesis and the RNA-seq data, suggesting that tetrapyrrole chromophore biosynthesis and chlorophyll metabolism are mainly in the chloroplast in Cucumis sativus | Cucumis sativus |