(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) > cellular organisms: NE > Eukaryota: NE > Viridiplantae: NE > Streptophyta: NE > Streptophytina: NE > Embryophyta: NE > Tracheophyta: NE > Euphyllophyta: NE > Spermatophyta: NE > Magnoliophyta: NE > Mesangiospermae: NE > eudicotyledons: NE > Gunneridae: NE > Pentapetalae: NE > rosids: NE > malvids: NE > Brassicales: NE > Brassicaceae: NE > Brassiceae: NE > Brassica: NE > Brassica oleracea: NE
Bodyguard : braol-a0a3p6h726Brassica oleracea (Wild cabbage, Mustard); Brassica cretica Uncharacterized protein. Chlorophyllase_Plant : braol-Q8GTM4Brassica oleracea (Cauliflower), Brassica rapa, Brassica napus, chlorophyllase 1 (EC 3.1.1.14). FSH1 : braol-a0a3p6epu0Brassica oleracea (Wild cabbage). FSH1 domain-containing protein. Palmitoyl-protein_thioesterase : braol-q2a9a2Brassica oleracea (Wild cabbage) palmitoyl protein thioesterase family protein, braol-q2a9c0Brassica oleracea (Wild cabbage) palmitoyl protein thioesterase family protein, braol-q2a9i7Brassica oleracea (Wild cabbage) palmitoyl protein thioesterase family protein, braol-q2a9s0Brassica oleracea (Wild cabbage) palmitoyl protein thioesterase family protein
Warning: This entry is a compilation of different species or line or strain with more than 90% amino acid identity. You can retrieve all strain data
(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) Brassica oleracea var. oleracea: N, E.
Brassica oleracea var. medullosa: N, E.
Brassica oleracea var. italica: N, E.
Brassica oleracea var. botrytis: N, E.
Brassica oleracea var. alboglabra: N, E.
Brassica rapa subsp. pekinensis: N, E.
Brassica napus: N, E.
Brassica napus var. napus: N, E.
LegendThis sequence has been compared to family alignement (MSA) red => minority aminoacid blue => majority aminoacid color intensity => conservation rate title => sequence position(MSA position)aminoacid rate Catalytic site Catalytic site in the MSA MSSSSSRNAFVDGKYKPDLLTVDLASRCRCYKTTPSSSLTPPPPPKSLLV ATPVEEGEYPVVMLLHGYLLYNSFYSQLMLHVSSYGFIVIAPQLYNIAGP DTIDEIKSTAEIIDWLSVGLNHFLPPQVTPNLSKFALTGHSRGGKTAFAV ALKKFGYSSELKISAIIGVDPVDGTGKGKQTPPPVLTYEPNSFNLEKMPV LVIGSGLGELARNPLFPPCAPTGVNHREFFQECQGPAWHFVAKDYGHLDM LDDDTKGLRGKSSYCLCKNGEERKPMRRFIGGIVVSFLMAYLEDDDCELV KIKAGCHEGVPVEIQEFEVKK
Oilseed rape (Brassica napus L.) was formed ~7500 years ago by hybridization between B. rapa and B. oleracea, followed by chromosome doubling, a process known as allopolyploidy. Together with more ancient polyploidizations, this conferred an aggregate 72x genome multiplication since the origin of angiosperms and high gene content. We examined the B. napus genome and the consequences of its recent duplication. The constituent An and Cn subgenomes are engaged in subtle structural, functional, and epigenetic cross-talk, with abundant homeologous exchanges. Incipient gene loss and expression divergence have begun. Selection in B. napus oilseed types has accelerated the loss of glucosinolate genes, while preserving expansion of oil biosynthesis genes. These processes provide insights into allopolyploid evolution and its relationship with crop domestication and improvement.
We report the annotation and analysis of the draft genome sequence of Brassica rapa accession Chiifu-401-42, a Chinese cabbage. We modeled 41,174 protein coding genes in the B. rapa genome, which has undergone genome triplication. We used Arabidopsis thaliana as an outgroup for investigating the consequences of genome triplication, such as structural and functional evolution. The extent of gene loss (fractionation) among triplicated genome segments varies, with one of the three copies consistently retaining a disproportionately large fraction of the genes expected to have been present in its ancestor. Variation in the number of members of gene families present in the genome may contribute to the remarkable morphological plasticity of Brassica species. The B. rapa genome sequence provides an important resource for studying the evolution of polyploid genomes and underpins the genetic improvement of Brassica oil and vegetable crops.
Postharvest yellowing in broccoli is known to result from chlorophyll degradation, with chlorophyllase the first enzyme to degrade chlorophyll. In broccoli, three putative chlorophyllase genes (BoCLH1, BoCLH2, and BoCLH3) were cloned using degenerate primers from the conserved regions of known chlorophyllases. Among these three genes, only BoCLH1 is transcribed during the course of broccoli postharvest senescence. A chimeric construct with the antisense BoCLH1, driven by the CaMV 35S promoter and Nos-terminator and harboring the hygromycin resistance gene, was used for Agrobacterium-mediated transformation to study the effects of the antisense BoCLH1 gene on the postharvest senescence of broccoli. From a total of about 90 primary transformants, 35 individuals were selected and grown for further studies, with 22 of these grown to maturity. Based on the Chl retention rate on Days 4 and 5, respectively, 45% of the detached florets and over 60% of the detached leaves of the selected transformants exhibited slower yellowing when stored at 20C in darkness. Southern blot analyses were conducted to eliminate the possible non-independent transformants and investigate the insertion patterns and copy numbers. Only a few lines with simple insertion site and copy number and postharvest yellowing retardation effects were self-pollintated for further evaluation. Northern analyses showed antisense BoCLH1 mRNA transcripts on the day of harvest, the levels of which gradually decreased 4-5 days postharvest when stored at 20C in darkness. Positive correlations between the antisense BoCLH1 transcripts and slower postharvest yellowing were noted in some selected lines. Only 1-2 days delay in yellowing was observed in the selected antisense BoCLH1-positive transformants. No individual antisense BoCLH2 or BoCLH3 transformants showed significant slowing of postharvest yellowing. The results suggested genes other than the BoCLH-Chlases obtained in the present study might also be essential in the yellowing process.
