THE BIFUNCTIONAL PROTEIN DCOH PCD, A TRANSCRIPTION FACTOR WITH A CYTOPLASMIC ENZYMATIC-ACTIVITY, IS A MATERNAL FACTOR IN THE RAT EGG AND EXPRESSED TISSUE SPECIFICALLY DURING EMBRYOGENESIS/
Epv. Strandmann et al., THE BIFUNCTIONAL PROTEIN DCOH PCD, A TRANSCRIPTION FACTOR WITH A CYTOPLASMIC ENZYMATIC-ACTIVITY, IS A MATERNAL FACTOR IN THE RAT EGG AND EXPRESSED TISSUE SPECIFICALLY DURING EMBRYOGENESIS/, The International journal of developmental biology, 42(1), 1998, pp. 53-59
The bifunctional protein DCoH/PCD is both a cytoplasmatic enzyme (PCD)
involved in the tetrahydrobiopterin regeneration and a transcription
coactivator (DCoH). Originally detected in liver cell nuclei, it forms
a 2:2 heterotetrametric complex with the nuclear transcription factor
s HNF1 alpha and the variant form HNF1 beta and enhances their transcr
iptional potential. To address the role of DCoH in tissue specific and
developmental gene regulation we analyzed its spatial and temporal ex
pression pattern in the rat. DCoH might have a function in tissue spec
ific gene expression mediated by HNF1 in the adults and in the develop
ing embryo as it is found in the kidney and the liver, organs known to
contain HNF1. In addition DCoH is a maternal factor in the rat egg la
cking HNF1 transcription factors. The maternal protein enters the cell
nuclei at the 8-cell stage suggesting a role in early embryonic gene
regulation and excluding a cytoplasmatic enzymatic function. Evidence
for a HNF1 independent function of DCoH is also given by the fact that
DCoH is present in the eyes (pigmented epithelium) and the brain (epe
ndym cells) of the rat embryos, cell types lacking HNF1 proteins. The
tightly regulated expression pattern of DCoH in distinct cell types or
iginating from endo- meso- and ectoderm is conserved between the rat a
nd the frog indicating a fundamental role for DCoH in early gene regul
ation among the vertebrates.