Development Genes and Evolution

Boyan, George; Liu, Yu

doi: 10.1007/s00427-013-0462-8pmid: 24343526

This study employs labels for cell proliferation and cell death, as well as classical histology to examine the fates of all eight neural stem cells (neuroblasts) whose progeny generate the central complex of the grasshopper brain during embryogenesis. These neuroblasts delaminate from the neuroectoderm between 25 and 30 % of embryogenesis and form a linear array running from ventral (neuroblasts Z, Y, X, and W) to dorsal (neuroblasts 1-2, 1-3, 1-4, and 1-5) along the medial border of each protocerebral hemisphere. Their stereotypic location within the array, characteristic size, and nuclear morphologies, identify these neuroblasts up to about 70 % of embryogenesis after which cell shrinkage and shape changes render progressively more cells histologically unrecognizable. Molecular labels show all neuroblasts in the array are proliferative up to 70 % of embryogenesis, but subsequently first the more ventral cells (72–75 %), and then the dorsal ones (77–80 %), cease proliferation. By contrast, neuroblasts elsewhere in the brain and optic lobe remain proliferative. Apoptosis markers label the more ventral neuroblasts first (70–72 %), then the dorsal cells (77 %), and the absence of any labeling thereafter confirms that central complex neuroblasts have exited the cell cycle via programmed cell death. Our data reveal appearance, proliferation, and cell death proceeding as successive waves from ventral to dorsal along the array of neuroblasts. The resulting timelines offer a temporal blueprint for building the neuroarchitecture of the various modules of the central complex.

Morris, Valerie B.; Byrne, Maria

doi: 10.1007/s00427-013-0457-5pmid: 24129745

Hox genes are noted for their roles in specifying axial identity in bilateral forms. In the radial echinoderms, the axis whose identity Hox genes might specify remains unclear. From the expression of Hox genes in the development of the sea urchin Holopneustes purpurescens reported here and that reported previously, we clarify the axis that might be specified by Hox genes in echinoderms. The expression of HpHox11/13 here is described at three developmental stages. The expression is around the rim of the blastopore in gastrulae, in the archenteron wall and adjacent mesoderm in early vestibula larvae, and in a patch of mesoderm close to the archenteron wall in later vestibula larvae. The retained expression of HpHox11/13 in the patch of mesoderm in the later vestibula larvae is, we suggest, indicative of a posterior or an aboral growth zone. The expression of HpHox3 at the echinoid-rudiment stage, in contrast, is in oral mesoderm beneath the epineural folds, concentrated in sites where the first three adult spines form. With the expression of HpHox5 and HpHox11/13 reported previously, the expressions here support the role of Hox genes in specifying oral–aboral identity in echinoderms. How such specification and a posterior growth zone add support to a concept of the structural homology between echinoderms and chordates is discussed.

Kunii, Mizuho; Yasuno, Mami; Shindo, Yuki; Kawata, Takefumi

doi: 10.1007/s00427-013-0460-xpmid: 24240571

Dictyostelium discoideum is a facultative multicellular amoebozoan with cellulose in the stalk and spore coat of its fruiting body as well as in the extracellular matrix of the migrating slug. The organism also harbors a number of cellulase genes. One of them, cbhA, was identified as a candidate cellobiohydrolase gene based on the strong homology of its predicted protein product to fungal cellobiohydrolase I (CBHI). Expression of the cbhA was developmentally regulated, with strong expression in the spores of the mature fruiting body. However, a weak but detectable level of expression was observed in the extracellular matrix at the mound — tipped finger stages, in prestalk O cells, and in the slime sheath of the migrating slug — late culminant stages. A null mutant of the cbhA showed almost normal morphology. However, the developmental timing of the mutant was delayed by 2–4 h. When a c-Myc epitope-tagged CbhA was expressed, it was secreted into the culture medium and was able to bind crystalline cellulose. The CbhA-myc protein was glycosylated, as demonstrated by its ability to bind succinyl concanavalin A-agarose. Moreover, conditioned medium from the cbhA-mycoe strain displayed 4-methylumbelliferyl β-d-cellobioside (4-MUC) digesting activity in Zymograms in which conditioned medium was examined via native-polyacrylamide gel electrophoresis or spotted on an agar plate containing 4-MUC, one of the substrates of cellobiohydrolase. Taken together, these findings indicate that Dictyostelium CbhA is an orthologue of CBH I that is required for a normal rate of development.

Yuwen, Yanqing; Dong, Zimei; Si, Xiaohui; Chen, Guangwen

doi: 10.1007/s00427-013-0459-3pmid: 24292205

Pumilio proteins (PUMs), members of the pumilio/fem-3 mRNA-binding factor (PUF) family, are eukaryote-specific RNA-binding proteins. We isolated a 2,048-basepair cDNA fragment of a pumilio homolog from the planarian flatworm Polycelis sp. This pumilio protein (PyPUM) contains a conserved pumilio homology domain (PUM-HD) consisting of eight repeats and two flanking half repeats. PyPUM shows high similarity to Dugesia japonica pumilio (DjPUM) from another planarian D. japonica, and their PUM-HD also shows high similarity to each other. Furthermore, our data showed that there is a flatworm-specific spacer between repeats 7 and 8. Phylogenetic analysis showed that PyPUM has a closer relationship to other PUM homologs from flatworms. These results provide a foundation for future functional studies of pumilio gene in Polycelis sp.

Sun, Yanqi; Pu, Zongjun; Dai, Shoufen; Pu, Xiaoxue; Liu, Dengcai; Wu, Bihua; Lan, Xiujin; Wei, Yuming; Zheng, Youliang; Yan, Zehong

doi: 10.1007/s00427-013-0455-7pmid: 24068388

Three y-type high-molecular-weight (HMW) glutenin gene open reading frames (ORFs), Chiy1, Chiy2, and Racy, were isolated and characterized from Leymus chinensis PI499516 and Leymus racemosus ssp. racemosus W623305. They shared an extra glutamine in the N-terminal and LAAQLPAMCRL peptides in the C-terminal with x-type HMW glutenins but had different N-terminal lengths. Like other y-type HMW glutenins, Chiy2 and Racy had 104 (or 105) amino acid (aa) residues at the N-terminal and started with EGEASR, whereas Chiy1 had 99 aa in this domain and started with QLQCER because of the deletion of EGEASR. Five other y-type glutenins, including those from Elymus ciliaris, Pseudoroegneria libanotica, and Leymus mollis, were similar to Chiy1. The ORF of Chiy2 was probably not expressed. The ORFs of both Chiy1 and Racy were expressed in bacteria. The maximum likelihood phylogenic tree based on the signal peptide and N-terminal and C-terminal aa residues revealed two clades of y-type HMW glutenins in Triticeae; the first contained Ay, By, Cy, Dy, Eey, Gy, Ky, Ry, Tay, and Uy, while the second clade contained the remaining y types, including those from Leymus. Within the second clade, HMW glutenins lacking the EGEASR peptide formed a subclade. These y-type HMW glutenins in Leymus could not be targeted to the Xm or Ns genome.