So what part of dicty other than the Dd is used? and how?
ABSTRACT
We have cloned and characterized the Dictyostelium
discoideum repE gene, a homolog of the human
xeroderma pigmentosum (XP) group E gene which
encodes a UV-damaged DNA binding protein. The repE
gene maps to chromosome 4 and it is the first gene
identified in Dictyostelium that is homologous to those
involved in nucleotide excision repair and their related
XP diseases in humans. The predicted protein
encodes a leucine zipper motif. The repE gene is not
expressed by mitotically dividing cells, and repE
mRNA is first detected during the aggregation phase of
development when the cells have ceased dividing and
replicating genomic DNA. The mRNA level plateaus by
the time the developing cells have entered multicellular
aggregates and remains at the same steady-state level
for the remainder of development. In addition, we have
demonstrated that the level of mRNA is very low in
developing cells. These observations suggest that
repE may play a regulatory role in development. The
data indicate that potential developmental roles for
XP-related genes can be profitably studied in this
system.
nar.oxfordjournals.org/cgi/reprint/24/12/2295.pdf===============
If this is a homologue that means it is similar to human gene so can be used
to change or integrate into gene as gene therapy like in the drug itself,
given another name. You have no idea it is used in the drug.
Dimers formed from UV radiation, perpetuated by chemtrails, not sun, and then
drug created to stop the pigment problems.
wonder if dimers are mentioned in this construction?
================
Abstract
We describe a Dictyostelium STAT, Dd-STATc, which regulates the speed of early development and the timing of terminal differentiation. Dd-STATc also functions as a repressor, which directs graded expression of the ecmA gene in different prestalk cell populations. Developing Dictyostelium cells produce a chlorinated hexaphenone, DIF, which directs prestalk cell differentiation.
Dd-STATc is tyrosine phosphorylated, dimerizes, and translocates to the nucleus when cells are exposed to DIF. Surprisingly, however, SH2 domain–phosphotyrosine interaction is not necessary for the DIF-induced nuclear translocation of Dd-STATc. In this respect, Dd-STATc activation resembles several recently described, noncanonical mammalian STAT signaling processes. We show instead that DIF mediates nuclear translocation via sequences located in the divergent, N-terminal half of the Dd-STATc molecule.
linkinghub.elsevier.com/retrieve/pii/S1097276501002222The Extra cellular matrix;
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Cell Junctions, Cell Adhesion, and the Extracellular Matrix
........"After Secretion Fibrillar Procollagen Molecules Are Cleaved to Collagen Molecules, Which Assemble into Fibrils 23, 24, 25
After secretion the propeptides of the fibrillar procollagen molecules are removed by specific proteolytic enzymes outside the cell. This converts the procollagen molecules to collagen molecules, which assemble in the extracellular space to form much larger collagen fibrils. The propeptides have at least two functions: (1) they guide the intracellular formation of the triple-stranded collagen molecules, and (2) because they are removed only after secretion, they prevent the intracellular formation of large collagen fibrils, which could be catastrophic for the cell. The process of fibril formation is driven, in part, by the tendency of the collagen molecules, which are more than 1000-fold less soluble than procollagen molecules, to self-assemble. The fibrils begin to form close to the cell surface, often in deep infoldings of the plasma membrane formed by the tandem fusion of secretory vesicles with the cell surface. The underlying cortical cytoskeleton can therefore influence the sites, rates, and orientation of fibril assembly.
Figure 19-43 summarizes the various steps in the synthesis and assembly of collagen fibrils. Given the large number of enzymatic steps involved in forming a collagen fibril, it is not surprising that there are many human genetic diseases that affect fibril formation. Mutations affecting type I collagen cause osteogenesis imperfecta, characterized by weak bones that easily fracture. Mutations affecting type II collagen cause chondrodysplasias, characterized by abnormal cartilage, which leads to bone and joint deformities. Mutations affecting type III collagen cause Ehlers-Danlos syndrome, characterized by fragile skin and blood vessels and hypermobile joints."..............
www.ncbi.nlm.nih.gov/bookshelf/br.fcgi?book=cell&part=A5085gotta wade through this one.
skyship