Expression profile of cuticular genes of silkworm, Bombyx mori

<p>Abstract</p> <p>Background</p> <p>Insect cuticle plays essential roles in many physiological functions. During molting and metamorphosis tremendous changes occur in silkworm cuticle where multiple proteins exist and genes encoding them constitute about 1.5% of all <it>Bombyx mori </it>genes.</p> <p>Results</p> <p>In an effort to determine their expression profiles, a microarray-based investigation was carried out using mRNA collected from larvae to pupae. The results showed that a total of 6676 genes involved in various functions and physiological pathways were activated. The vast majority (93%) of cuticular protein genes were expressed in selected stages with varying expression patterns. There was no correlation between expression patterns and the presence of conserved motifs. Twenty-six RR genes distributed in chromosome 22 were co-expressed at the larval and wandering stages. The 2 kb upstream regions of these genes were further analyzed and three putative elements were identified.</p> <p>Conclusions</p> <p>Data from the present study provide, for the first time, a comprehensive expression profile of genes in silkworm epidermal tissues and evidence that putative elements exist to allow massive production of mRNAs from specific cuticular protein genes.</p

Draft genome sequence of the mulberry tree Morus notabilis

Human utilization of the mulberry–silkworm interaction started at least 5,000 years ago and greatly influenced world history through the Silk Road. Complementing the silkworm genome sequence, here we describe the genome of a mulberry species Morus notabilis. In the 330-Mb genome assembly, we identify 128 Mb of repetitive sequences and 29,338 genes, 60.8% of which are supported by transcriptome sequencing. Mulberry gene sequences appear to evolve ~3 times faster than other Rosales, perhaps facilitating the species’ spread worldwide. The mulberry tree is among a few eudicots but several Rosales that have not preserved genome duplications in more than 100 million years; however, a neopolyploid series found in the mulberry tree and several others suggest that new duplications may confer benefits. Five predicted mulberry miRNAs are found in the haemolymph and silk glands of the silkworm, suggesting interactions at molecular levels in the plant–herbivore relationship. The identification and analyses of mulberry genes involved in diversifying selection, resistance and protease inhibitor expressed in the laticifers will accelerate the improvement of mulberry plants

Additional file 7: Figure S6. of Evolutionary and functional analysis of mulberry type III polyketide synthases

The subcellular localization of mulberry type III polyketide synthases. (A) The control vector pLGNL-EGFP, (B) pLGNL-MnPKS1-EGFP, (C) pLGNL-MnPKS2-EGFP, (D) pLGNL-MnCHS2-EGFP, (E) pLGNL-MnCHS6-EGFP, (G) pLGNL-MnSTS7-EGFP, and (F) pLGNL-MnSTS8-EGFP were transiently expressed in tobacco epidermal cells. Column (a), bright filed; column (b), EGFP fluorescence; and column (c), merged fluorescence. (PDF 3312 kb

Additional file 3: Figure S2. of Evolutionary and functional analysis of mulberry type III polyketide synthases

Comparison of mulberry type III polyketide synthase amino acid sequences. Conserved sites are shaded. The asterisk indicates the site contains a conserved Thr197 in CHS, but a Gly in PKS1 and PKS2. Purple arrow: positive selection and type II divergence sites; red arrow: positive selection sites; green arrow: type I divergence sites; yellow arrow: type II divergence sites. Red box: catalytic triad; blue box: co-enzyme A binding sites; yellow box: important residues for functional diversity. (PDF 2015 kb

[Adenophora sp.]

原著和名: [記載なし]科名: キキョウ科 = Campanulaceae採集地: 北海道 磯谷郡 蘭越町 港町 (北海道 後志 蘭越町 港町)採集日: 1974/7/21採集者: 萩庭丈壽整理番号: JH023564国立科学博物館整理番号: TNS-VS-973564備考: DB作成協力会による補足あ

Alangium premnifolium Ohwi

原著和名: シマウリノキ科名: ウリノキ科 = Alangiaceae採集地: 鹿児島県 種子島 中種子町 浜津脇 (大隅 種子島 中種子町 浜津脇)採集日: 1970/8/4採集者: 萩庭丈壽整理番号: JH024376国立科学博物館整理番号: TNS-VS-97437

Uncovering the functional residues of Arabidopsis isoprenoid biosynthesis enzyme HDS

The methylerythritol phosphate (MEP) pathway is responsible for producing isoprenoids, metabolites with essential functions in the bacterial kingdom and plastid-bearing organisms including plants and Apicomplexa. Additionally, the MEP-pathway intermediate methylerythritol cyclodiphosphate (MEcPP) serves as a plastid-to-nucleus retrograde signal. A suppressor screen of the high MEcPP accumulating mutant plant (ceh1) led to the isolation of 3 revertants (designated Rceh1-3) resulting from independent intragenic substitutions of conserved amino acids in the penultimate MEP-pathway enzyme, hydroxymethylbutenyl diphosphate synthase (HDS). The revertants accumulate varying MEcPP levels, lower than that of ceh1, and exhibit partial or full recovery of MEcPP-mediated phenotypes, including stunted growth and induced expression of stress response genes and the corresponding metabolites. Structural modeling of HDS and ligand docking spatially position the substituted residues at the MEcPP binding pocket and cofactor binding domain of the enzyme. Complementation assays confirm the role of these residues in suppressing the ceh1 mutant phenotypes, albeit to different degrees. In vitro enzyme assays of wild type and HDS variants exhibit differential activities and reveal an unanticipated mismatch between enzyme kinetics and the in vivo MEcPP levels in the corresponding Rceh lines. Additional analyses attribute the mismatch, in part, to the abundance of the first and rate-limiting MEP-pathway enzyme, DXS, and further suggest MEcPP as a rheostat for abundance of the upstream enzyme instrumental in fine-tuning of the pathway flux. Collectively, this study identifies critical residues of a key MEP-pathway enzyme, HDS, valuable for synthetic engineering of isoprenoids, and as potential targets for rational design of antiinfective drugs